CLPX_BACSU
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 03-AUG-2022, entry version 153.
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}; 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], AND INDUCTION BY STRESS.
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 gene
RT of Bacillus subtilis.";
RL Gene 181:77-83(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
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 subtilis
RT chromosome containing genes responsible for stress responses, the
RT 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., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., 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., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., 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., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 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.
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / Marburg / 1012;
RX PubMed=11395451; DOI=10.1128/jb.183.13.3885-3889.2001;
RA Wiegert T., Schumann W.;
RT "SsrA-mediated tagging in Bacillus subtilis.";
RL J. Bacteriol. 183:3885-3889(2001).
CC -!- FUNCTION: ATP-dependent specificity component of the Clp protease. It
CC directs the protease to specific substrates. Can perform chaperone
CC functions in the absence of ClpP (By similarity). Probably the major
CC protease that degrades proteins tagged by trans-translation
CC (PubMed:11395451). {ECO:0000255|HAMAP-Rule:MF_00175,
CC ECO:0000269|PubMed:11395451}.
CC -!- SUBUNIT: Component of the ClpX-ClpP complex. Forms a hexameric ring
CC that, in the presence of ATP, binds to fourteen ClpP subunits assembled
CC into a disk-like structure with a central cavity, resembling the
CC structure of eukaryotic proteasomes. {ECO:0000255|HAMAP-Rule:MF_00175}.
CC -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:8973311}.
CC -!- DISRUPTION PHENOTYPE: No degradation of trans-translationally tagged-
CC peptides. {ECO:0000269|PubMed:11395451}.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000255|HAMAP-
CC 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 AlphaFoldDB; P50866; -.
DR SMR; P50866; -.
DR IntAct; P50866; 1.
DR MINT; P50866; -.
DR STRING; 224308.BSU28220; -.
DR jPOST; P50866; -.
DR PaxDb; P50866; -.
DR PRIDE; P50866; -.
DR EnsemblBacteria; CAB14782; CAB14782; BSU_28220.
DR GeneID; 937482; -.
DR KEGG; bsu:BSU28220; -.
DR PATRIC; fig|224308.179.peg.3065; -.
DR eggNOG; COG1219; Bacteria.
DR InParanoid; P50866; -.
DR OMA; HYKRVQA; -.
DR PhylomeDB; P50866; -.
DR BioCyc; BSUB:BSU28220-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0009376; C:HslUV protease complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0030163; P:protein catabolic process; IMP:CACAO.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 6.20.220.10; -; 1.
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; IPR046425; ClpX_bact.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010603; Znf_CppX_C4.
DR InterPro; IPR038366; Znf_CppX_C4_sf.
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.
DR PROSITE; PS51902; CLPX_ZB; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Metal-binding; Nucleotide-binding;
KW Reference proteome; Stress response; Zinc.
FT CHAIN 1..420
FT /note="ATP-dependent Clp protease ATP-binding subunit ClpX"
FT /id="PRO_0000160313"
FT DOMAIN 1..54
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 117..124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00175"
FT CONFLICT 109
FT /note="K -> Q (in Ref. 1; CAA64618 and 2; CAA99537)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="K -> E (in Ref. 1; CAA64618 and 2; CAA99537)"
FT /evidence="ECO:0000305"
FT CONFLICT 173..174
FT /note="AE -> TG (in Ref. 1; CAA64618 and 2; CAA99537)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="A -> R (in Ref. 2; CAA99537 and 5; AAA84743)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="G -> A (in Ref. 2; CAA99537 and 5; AAA84743)"
FT /evidence="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
