ID   HSCA_VIBC3              Reviewed;         616 AA.
AC   A5F3G8; C3LY62;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679};
GN   OrderedLocusNames=VC0395_A0281, VC395_0769;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
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; CP000627; ABQ21186.1; -; Genomic_DNA.
DR   EMBL; CP001235; ACP08786.1; -; Genomic_DNA.
DR   RefSeq; WP_001196560.1; NZ_JAACZH010000017.1.
DR   AlphaFoldDB; A5F3G8; -.
DR   SMR; A5F3G8; -.
DR   STRING; 345073.VC395_0769; -.
DR   PRIDE; A5F3G8; -.
DR   EnsemblBacteria; ABQ21186; ABQ21186; VC0395_A0281.
DR   GeneID; 57739462; -.
DR   KEGG; vco:VC0395_A0281; -.
DR   KEGG; vcr:VC395_0769; -.
DR   PATRIC; fig|345073.21.peg.743; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
DR   Proteomes; UP000000249; Chromosome 2.
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_1000072729"
SQ   SEQUENCE   616 AA;  65838 MW;  203EBF82CECDE7CC 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 TQAKIDLTEY MTAELNVLGW QGSLTREELE
     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 DELLNEQERQ TLLQAIERLI ELRNGDNADA IEQGIKDTDK ASQDFASRRM
     DKSIRSALAG HSVDEI