ID   HSCA_PSET1              Reviewed;         620 AA.
AC   Q3IFG5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=PSHAa2667;
OS   Pseudoalteromonas translucida (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C.,
RA   Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT   Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(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; CR954246; CAI87715.1; -; Genomic_DNA.
DR   RefSeq; WP_011329312.1; NC_007481.1.
DR   AlphaFoldDB; Q3IFG5; -.
DR   SMR; Q3IFG5; -.
DR   STRING; 326442.PSHAa2667; -.
DR   EnsemblBacteria; CAI87715; CAI87715; PSHAa2667.
DR   KEGG; pha:PSHAa2667; -.
DR   PATRIC; fig|326442.8.peg.2576; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_3_6; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   BioCyc; PHAL326442:PSHA_RS13120-MON; -.
DR   Proteomes; UP000006843; Chromosome I.
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_1000044873"
SQ   SEQUENCE   620 AA;  66364 MW;  EA8E274331B69EC9 CRC64;
     MALLQIAEPG QSAAPHEHKL AIGIDLGTTN SLVATVQSGE ARTLTDDLGE AMLPSVVRYQ
     AGGITVGSEA VKSATQDPVN TLISVKRFLG KTQAEIEQSY GQLPYQFCQH DGALAIETAA
     GKISPVKASS HILAALKARA EQSFGNQEIL GAVITVPAYF DDAQRQSTKD AAELAGINVL
     RLLNEPTAAA VAYGLDSGQE GIIAVYDLGG GTFDISILRL HQGVFEVLAT GGDSSLGGDD
     FDSLIVDYLK QQTGVTTLSP AVLRLFINKA KACKEALSQY STVNVGLEFD DEKHMVEVTR
     EKLDELAIPL VKKTLRSCRR AVKDAGIENE EVLQVIMVGG STRMPLVRSQ VSEFFNKEAL
     TSIDPDRVVA LGAALQADVL IGNKPDSDML LLDVLPLSLG LETMGGLVEK IIPRNTTIPV
     ARAQEFTTFK DGQTAMSLHV LQGERELVDD CRSLAKFSLK GIPPMTAGAA HIRVTFKVDA
     DGLLSVSAME KSTGVQADIQ VKPSFGLSDD QVSNMLKESM SNAKGDMQAR MLKEQQVEAL
     RVIEALEASL ASDSGLLDEA QLAYLRAEIA ELVKVRENAQ QPNEIKTAIE KMDNASSDFA
     ARRMDASIKK VLTGQSVDNI