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