ID   CLPX_BACSU              Reviewed;         420 AA.
AC   P50866;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 3.
DT   27-MAY-2015, entry version 115.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000255|HAMAP-Rule:MF_00175};
GN   Name=clpX {ECO:0000255|HAMAP-Rule:MF_00175};
GN   OrderedLocusNames=BSU28220;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8973311; DOI=10.1016/S0378-1119(96)00467-2;
RA   Gerth U., Wipat A., Harwood C.R., Carter N., Emmerson P.T., Hecker M.;
RT   "Sequence and transcriptional analysis of clpX, a class-III heat-shock
RT   gene of Bacillus subtilis.";
RL   Gene 181:77-83(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969504;
RA   Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA   Emmerson P.T., Harwood C.R.;
RT   "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus
RT   subtilis chromosome containing genes responsible for stress responses,
RT   the utilization of plant cell walls and primary metabolism.";
RL   Microbiology 142:3067-3078(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   SEQUENCE REVISION TO 109; 161; 174; 247 AND 260.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G.,
RA   Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus
RT   subtilis 168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 231-420.
RC   STRAIN=168;
RA   Ye R., Wong S.L.;
RL   Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATP-dependent specificity component of the Clp protease.
CC       It directs the protease to specific substrates. Can perform
CC       chaperone functions in the absence of ClpP. {ECO:0000255|HAMAP-
CC       Rule:MF_00175}.
CC   -!- SUBUNIT: Component of the ClpX-ClpP complex. Forms a hexameric
CC       ring that, in the presence of ATP, binds to fourteen ClpP subunits
CC       assembled into a disk-like structure with a central cavity,
CC       resembling the structure of eukaryotic proteasomes.
CC       {ECO:0000255|HAMAP-Rule:MF_00175}.
CC   -!- INDUCTION: By heat shock.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family.
CC       {ECO:0000255|HAMAP-Rule:MF_00175}.
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DR   EMBL; X95306; CAA64618.1; -; Genomic_DNA.
DR   EMBL; Z75208; CAA99537.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14782.2; -; Genomic_DNA.
DR   EMBL; U18229; AAA84743.1; -; Genomic_DNA.
DR   PIR; D69601; D69601.
DR   RefSeq; NP_390700.2; NC_000964.3.
DR   RefSeq; WP_003229613.1; NZ_JNCM01000036.1.
DR   ProteinModelPortal; P50866; -.
DR   SMR; P50866; 11-49, 61-407.
DR   IntAct; P50866; 1.
DR   MINT; MINT-8365067; -.
DR   STRING; 224308.BSU28220; -.
DR   PaxDb; P50866; -.
DR   PRIDE; P50866; -.
DR   EnsemblBacteria; CAB14782; CAB14782; BSU28220.
DR   GeneID; 937482; -.
DR   KEGG; bsu:BSU28220; -.
DR   PATRIC; 18977520; VBIBacSub10457_2949.
DR   GenoList; BSU28220; -.
DR   eggNOG; COG1219; -.
DR   HOGENOM; HOG000010093; -.
DR   InParanoid; P50866; -.
DR   KO; K03544; -.
DR   OMA; CGRQHPQ; -.
DR   OrthoDB; EOG625JZK; -.
DR   PhylomeDB; P50866; -.
DR   BioCyc; BSUB:BSU28220-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030163; P:protein catabolic process; IMP:CACAO.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_00175; ClpX; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010603; Znf_CppX_C4.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   Pfam; PF06689; zf-C4_ClpX; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SMART; SM00994; zf-C4_ClpX; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00382; clpX; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Complete proteome; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Stress response; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    420       ATP-dependent Clp protease ATP-binding
FT                                subunit ClpX.
FT                                /FTId=PRO_0000160313.
FT   ZN_FING      13     38       C4-type. {ECO:0000255|HAMAP-
FT                                Rule:MF_00175}.
FT   NP_BIND     117    124       ATP. {ECO:0000255|HAMAP-Rule:MF_00175}.
FT   CONFLICT    109    109       K -> Q (in Ref. 1; CAA64618 and 2;
FT                                CAA99537). {ECO:0000305}.
FT   CONFLICT    161    161       K -> E (in Ref. 1; CAA64618 and 2;
FT                                CAA99537). {ECO:0000305}.
FT   CONFLICT    173    174       AE -> TG (in Ref. 1; CAA64618 and 2;
FT                                CAA99537). {ECO:0000305}.
FT   CONFLICT    247    247       A -> R (in Ref. 2; CAA99537 and 5;
FT                                AAA84743). {ECO:0000305}.
FT   CONFLICT    260    260       G -> A (in Ref. 2; CAA99537 and 5;
FT                                AAA84743). {ECO:0000305}.
SQ   SEQUENCE   420 AA;  46350 MW;  9ADB3F134CAE08CC CRC64;
     MFKFNEEKGQ LKCSFCGKTQ DQVRKLVAGP GVYICDECIE LCTEIVEEEL GTEEEVEFKD
     VPKPQEIREI LNEYVIGQDQ AKKSLAVAVY NHYKRINSNS KVDDVELSKS NISLIGPTGS
     GKTLLAQTLA RILNVPFAIA DATSLTEAGY VGEDVENILL KLIQAADYDV EKAEKGIIYI
     DEIDKVARKS ENPSITRDVS GEGVQQALLK ILEGTVASVP PQGGRKHPHQ EFIQIDTTNI
     LFICGGAFDG IEQIIKRRLG QKVIGFGADN KAADLEKEDL LSKVLPEDLL RFGLIPEFIG
     RLPVIASLEK LDEEALVAIL TKPKNALVKQ FKKMLELDNV ELEFEEEALS EIAKKAIERK
     TGARGLRSII EGIMLDVMFE LPSRDDIEKC VITGATVTHG EPPRLLLKDG TEVSQDKTSA
//