ID   HSCA_VIBCM              Reviewed;         616 AA.
AC   C3LT05;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=VCM66_0710;
OS   Vibrio cholerae serotype O1 (strain M66-2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=579112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M66-2;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
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; CP001233; ACP05031.1; -; Genomic_DNA.
DR   RefSeq; WP_001196554.1; NC_012578.1.
DR   AlphaFoldDB; C3LT05; -.
DR   SMR; C3LT05; -.
DR   EnsemblBacteria; ACP05031; ACP05031; VCM66_0710.
DR   KEGG; vcm:VCM66_0710; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
DR   Proteomes; UP000001217; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding.
FT   CHAIN           1..616
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000190673"
SQ   SEQUENCE   616 AA;  65833 MW;  978C62BC14655EBB CRC64;
     MALLQIAEPG QSSAPHQHKL AAGIDLGTTN SLVASVRSGT ASTLVDSQGR SILPSVVNYG
     ADATRVGYPA REQAETDPHN TVISVKRLLG RSLQDINQRY PHLPYRFKAS EKGLPIVQTA
     QGDKNPIQIS ADILKALAER ATATLGGELA GVVITVPAYF DDAQRVATKD AAALAGLHVL
     RLLNEPTAAA IAYGLDSGQE GVIAVYDLGG GTFDISILRL SRGVFEVLAT GGDSALGGDD
     FDHLIADHLQ AQIGLTSLTA EQQRALINAA TQAKIDLTEH MTAELNVLGW QGTFTREELE
     NLIAPLLKKT LLSCRRALKD AGVEADEVLE VVMVGGSTRT PFVREQVGEF FGRTPLTSIN
     PDEVVAIGAA IQADILAGNK PDAEMLLLDV IPLSLGIETM GGLVEKIIPR NTTIPVARAQ
     EFTTFKDGQT AMSVHVVQGE REMVDDCRSL ARFSLKGIPP MAAGAAHIRV TYQVDADGLL
     SVTALEKSTG VQAEIQVKPS YGLSDDEVTQ MLKDSMAYAK EDMLARALAE QRVEADRVIE
     GLVSALQADG DELLSEQERQ TLLQAIERLI ELRNGDNADA IEQGIKDTDK ASQDFASRRM
     DKSIRSALAG HSVDEI