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HSCA_COLP3
ID   HSCA_COLP3              Reviewed;         620 AA.
AC   Q486Y6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=CPS_1136;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=34H / ATCC BAA-681;
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
CC   -!- FUNCTION: Chaperone involved in the maturation of iron-sulfur cluster-
CC       containing proteins. Has a low intrinsic ATPase activity which is
CC       markedly stimulated by HscB. {ECO:0000255|HAMAP-Rule:MF_00679}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00679}.
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DR   EMBL; CP000083; AAZ28180.1; -; Genomic_DNA.
DR   RefSeq; WP_011041973.1; NC_003910.7.
DR   AlphaFoldDB; Q486Y6; -.
DR   SMR; Q486Y6; -.
DR   STRING; 167879.CPS_1136; -.
DR   PRIDE; Q486Y6; -.
DR   EnsemblBacteria; AAZ28180; AAZ28180; CPS_1136.
DR   KEGG; cps:CPS_1136; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_3_6; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000547; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR   CDD; cd10236; HscA_like_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   HAMAP; MF_00679; HscA; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR042039; HscA_NBD.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   InterPro; IPR010236; ISC_FeS_clus_asmbl_HscA.
DR   PANTHER; PTHR19375; PTHR19375; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF100934; SSF100934; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR01991; HscA; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..620
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000044855"
SQ   SEQUENCE   620 AA;  66198 MW;  8B8AC9DD8C19868C CRC64;
     MALLQIAEPG QSTVPHEHRL AAGIDLGTTN SLIASVQSGN ASTLSDDQGR DILPSIVSYQ
     AGNVLVGQTA QALSIEDAQN TITSAKRLIG RSLKDIQSKY PSLPYEFCGD ENHPEIMTRQ
     GAVNPVQVSA EILKSLNLRA QAALGGELTG VVITVPAHFD DAQRQSTKDA AKLAGVSVLR
     LLNEPTAAAV AYGLDSGQEG VIAVYDLGGG TFDISILRLN KGVFEVLATG GDSALGGDDF
     DVVLVDYLVE QAGLVRPLSP SLERQLMQQA CFAKEQLTTK EEVDITISLD SDSDWKTSLT
     KAQLNKLISS LVNKTLRACR RTLKDADITI DEVIEVVMVG GSTRVPLVRS EVEKHFNKTP
     LTSIDPDKVV AIGAAIQADV LVGNKPDSDM LLLDVTPLSL GLETMGGLVE KVIPRNTTIP
     VAKAQEFTTF KDGQTAMAVH VLQGERELVE DCRSLARFEL RGIPAMTAGA AHIRVTFKVD
     ADGLLSVSAM EKSSGVESSI EVKPSFGLDD NQISQMIKDS MSNAADDMQA RMLKEQQVEA
     SRVIESVQAA LLADSKLLNS DEITVIENAI KSLAQVSQGQ EIKAIENALD KLNDSTAIFA
     ERRMDSSISE ALAGQAVDKI
 
 
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