CLPY_BACSU
ID CLPY_BACSU Reviewed; 467 AA.
AC P39778;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=ATP-dependent protease ATPase subunit ClpY;
GN Name=clpY; Synonyms=codX, hslU; OrderedLocusNames=BSU16160;
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 / JH642;
RX PubMed=7783641; DOI=10.1111/j.1365-2958.1995.tb02378.x;
RA Slack F.J., Serror P., Joyce E., Sonenshein A.L.;
RT "A gene required for nutritional repression of the Bacillus subtilis
RT dipeptide permease operon.";
RL Mol. Microbiol. 15:689-702(1995).
RN [2]
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 [3]
RP CATALYTIC ACTIVITY, FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=11179218; DOI=10.1093/emboj/20.4.734;
RA Kang M.S., Lim B.K., Seong I.S., Seol J.H., Tanahashi N., Tanaka K.,
RA Chung C.H.;
RT "The ATP-dependent CodWX (HslVU) protease in Bacillus subtilis is an N-
RT terminal serine protease.";
RL EMBO J. 20:734-742(2001).
CC -!- FUNCTION: ATPase subunit of a proteasome-like degradation complex; this
CC subunit has chaperone activity. {ECO:0000269|PubMed:11179218}.
CC -!- ACTIVITY REGULATION: ATPase activity is much induced upon complex
CC formation with ClpQ. {ECO:0000269|PubMed:11179218}.
CC -!- SUBUNIT: A double ring-shaped homohexamer of ClpQ is capped on each
CC side by a ring-shaped ClpY homohexamer. The assembly of the ClpQ/ClpY
CC complex is dependent on binding of ATP (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC {ECO:0000305}.
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DR EMBL; U13634; AAB03371.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13489.1; -; Genomic_DNA.
DR PIR; E69601; E69601.
DR RefSeq; NP_389498.1; NC_000964.3.
DR RefSeq; WP_003245556.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P39778; -.
DR SMR; P39778; -.
DR IntAct; P39778; 1.
DR MINT; P39778; -.
DR STRING; 224308.BSU16160; -.
DR jPOST; P39778; -.
DR PaxDb; P39778; -.
DR PRIDE; P39778; -.
DR EnsemblBacteria; CAB13489; CAB13489; BSU_16160.
DR GeneID; 936301; -.
DR KEGG; bsu:BSU16160; -.
DR PATRIC; fig|224308.179.peg.1756; -.
DR eggNOG; COG1220; Bacteria.
DR InParanoid; P39778; -.
DR OMA; KYGMIKT; -.
DR PhylomeDB; P39778; -.
DR BioCyc; BSUB:BSU16160-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:0008233; F:peptidase activity; IEA:InterPro.
DR GO; GO:0036402; F:proteasome-activating activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043335; P:protein unfolding; IEA:UniProtKB-UniRule.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00249; HslU; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR004491; HslU.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR48102:SF3; PTHR48102:SF3; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00390; hslU; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT CHAIN 1..467
FT /note="ATP-dependent protease ATPase subunit ClpY"
FT /id="PRO_0000160476"
FT BINDING 20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 62..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 417
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 467 AA; 52586 MW; BD97599B6FFEB8C6 CRC64;
MEKKPLTPRQ IVDRLDQYIV GQQNAKKAVA VALRNRYRRS LLDEKLKDEV VPKNILMMGP
TGVGKTEIAR RIAKLSGAPF IKIEATKFTE VGYVGRDVES MVRDLVETSV RLIKEEKMNE
VKEQAEENAN KRIVRLLVPG KKKQSGVKNP FEMFFGGSQP NGEDEAESQE EANIEEKRKR
MAHQLALGEL EDYYVTVEVE EQQPSMFDML QGSGMEQMGM NMQDALSGLM PKKKKRRKMT
VREARKVLTN EEASKLIDMD EVGQEAVQRA EESGIIFIDE IDKIAKNGGA SSSADVSREG
VQRDILPIVE GSTVVTKYGS VKTDHVLFIA AGAFHMAKPS DLIPELQGRF PIRVELNKLT
VDDFVRILVE PDNALLKQYQ ALLQTEGISL EFSDEAIHKI AEVAYHVNQD TDNIGARRLH
TILERLLEDL SFEAPDVTME KITITPQYVE EKLGTIAKNK DLSQFIL
