ID   HSCA_VIBC1              Reviewed;         617 AA.
AC   A7MU49;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679};
GN   OrderedLocusNames=VIBHAR_01059;
OS   Vibrio campbellii (strain ATCC BAA-1116).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=2902295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1116 / BB120;
RG   The Vibrio harveyi Genome Sequencing Project;
RA   Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA   Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA   Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA   Wilson R.K.;
RL   Submitted (AUG-2007) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000789; ABU70052.1; -; Genomic_DNA.
DR   RefSeq; WP_012127088.1; NC_022269.1.
DR   AlphaFoldDB; A7MU49; -.
DR   SMR; A7MU49; -.
DR   EnsemblBacteria; ABU70052; ABU70052; VIBHAR_01059.
DR   KEGG; vha:VIBHAR_01059; -.
DR   PATRIC; fig|338187.25.peg.1569; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000008152; 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..617
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000044902"
SQ   SEQUENCE   617 AA;  66100 MW;  7EB2319B4BB0B485 CRC64;
     MALLQIAEPG QSSAPHEHKL AAGIDLGTTN SLVASVRSGD AKTLTDDQGR SILPSVVNYA
     QDTALVGYEA KAKAEQEPEN TIISVKRLIG RSLKDIQARY PSLPYQFKES DNGLPILQTA
     QGDKNPIEVS ADILKSLGKR AEETLGGELA GVVITVPAYF DDAQRAGTKD AAKLAGLHVL
     RLLNEPTAAA IAYGLDSGQE GVIAVYDLGG GTFDISILRL SKGVFEVLAT GGDSALGGDD
     FDHLLADYLM EQAGLEAPLS AEKNRALLNI ATATKIAFSE QDCVDVDVFG WKGAVTREQF
     EELIRPLVKK TLMSCRRALK DADVDAEDVL EAVMVGGSTR TLLVREMVGE FFGRTPLTSI
     NPDEVVAIGA GIQADILAGN KPDSEMLLLD VIPLSLGIET MGGLVEKIIP RNTTIPVARA
     QEFTTFKDGQ TAMSVHTVQG EREMVDDCRS LARFSLKGIP PMVAGAAHIR VTYQVDADGL
     LSVTAMEKST GVQAEIQVKP SYGLSDDEVA NMLRDSMTYA KEDMQARALA EQRVEADRVI
     EGLIAAMQAD GDELLSDQEK QDLVKVIEAL IELRNGEDAD AIEQGIKDTD KASQDFASRR
     MDKSIRAALS GQSVNDI