ID   HSCA_VIBA3              Reviewed;         616 AA.
AC   B7VJT0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=VS_0611;
OS   Vibrio atlanticus (strain LGP32) (Vibrio splendidus (strain Mel32)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=575788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LGP32;
RA   Mazel D., Le Roux F.;
RT   "Vibrio splendidus str. LGP32 complete genome.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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; FM954972; CAV17604.1; -; Genomic_DNA.
DR   RefSeq; WP_012603311.1; NC_011753.2.
DR   AlphaFoldDB; B7VJT0; -.
DR   SMR; B7VJT0; -.
DR   STRING; 575788.VS_0611; -.
DR   PRIDE; B7VJT0; -.
DR   EnsemblBacteria; CAV17604; CAV17604; VS_0611.
DR   KEGG; vsp:VS_0611; -.
DR   PATRIC; fig|575788.5.peg.1964; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000009100; Chromosome 1.
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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..616
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000190674"
SQ   SEQUENCE   616 AA;  65979 MW;  5FAE9786CB315E84 CRC64;
     MALLQIAEPG QSAAPHQQKL AVGIDLGTTN SLVAAVRSGE ASTLVDQQGR SILPSVVHYT
     SVSYTTGDEA RANAQTDPKN TIISVKRLIG RSLSDIQQRY PSLPYQFEES DNGLPVIRTE
     QGNKNPIQVS SDILRALGQR AESTLGGELS GAVITVPAYF DDAQRAGTKD AAQLAGLHVL
     RLLNEPTAAA IAYGLDSGKE GVIAVYDLGG GTFDISILRL SKGVFEVLAT GGDSALGGDD
     FDHLIAEHFQ EQMGLSELTA EQNRILLDAA TEAKIGLSEA ESVNVEVLGW AGSLTREEFE
     DIIKPLVKKT LLSCRRALKD AEVDADDVLE VVMVGGSTRT LLVREMVGDF FGRTPLTSIN
     PDEVVAIGAS IQADILVGNK PDSEMLLLDV IPLSLGIETM GGLVEKIIPR NTTIPVARAQ
     EFTTFKDGQT AMTVHTVQGE REMVDDCRSL ARFALKGIPP MAAGAAHIRV TYQVDADGLL
     SVTAMEKSTG VQAEIQVKPS YGLSDNEVAS MLKDSMTFAK EDMQARALAE QRVEADRVIE
     GLIAAMQADG DELLDEQEKQ HLLQAIEALI EVRNGESADA IELEIKNTDK ASQDFASRRM
     DKSIRAALSG QSVDNI