ID   HSCA_VIBCH              Reviewed;         616 AA.
AC   Q9KTX8;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=VC_0752;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
CC   -!- FUNCTION: Probable chaperone. Has a low intrinsic ATPase activity which
CC       is markedly stimulated by HscB (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00679}.
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DR   EMBL; AE003852; AAF93917.1; -; Genomic_DNA.
DR   PIR; C82286; C82286.
DR   RefSeq; NP_230401.1; NC_002505.1.
DR   RefSeq; WP_001196560.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KTX8; -.
DR   SMR; Q9KTX8; -.
DR   STRING; 243277.VC_0752; -.
DR   PRIDE; Q9KTX8; -.
DR   DNASU; 2615761; -.
DR   EnsemblBacteria; AAF93917; AAF93917; VC_0752.
DR   GeneID; 57739462; -.
DR   KEGG; vch:VC_0752; -.
DR   PATRIC; fig|243277.26.peg.716; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
DR   BioCyc; VCHO:VC0752-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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_0000078651"
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