ID A0A1E5E5I8_9VIBR Unreviewed; 616 AA.
AC A0A1E5E5I8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000256|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000256|HAMAP-Rule:MF_00679};
GN ORFNames=A1QC_04960 {ECO:0000313|EMBL:OEF28620.1};
OS Vibrio rumoiensis 1S-45.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1188252 {ECO:0000313|EMBL:OEF28620.1, ECO:0000313|Proteomes:UP000094070};
RN [1] {ECO:0000313|EMBL:OEF28620.1, ECO:0000313|Proteomes:UP000094070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1S-45 {ECO:0000313|EMBL:OEF28620.1,
RC ECO:0000313|Proteomes:UP000094070};
RX PubMed=22955834; DOI=10.1126/science.1219385;
RA Cordero O.X., Wildschutte H., Kirkup B., Proehl S., Ngo L., Hussain F.,
RA Le Roux F., Mincer T., Polz M.F.;
RT "Ecological populations of bacteria act as socially cohesive units of
RT antibiotic production and resistance.";
RL Science 337:1228-1231(2012).
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:0000256|HAMAP-Rule:MF_00679}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|HAMAP-Rule:MF_00679,
CC ECO:0000256|RuleBase:RU003322}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OEF28620.1}.
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DR EMBL; AJYK02000017; OEF28620.1; -; Genomic_DNA.
DR RefSeq; WP_017024460.1; NZ_AJYK02000017.1.
DR AlphaFoldDB; A0A1E5E5I8; -.
DR STRING; 1188252.A1QC_04960; -.
DR eggNOG; COG0443; Bacteria.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000094070; Unassembled WGS sequence.
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; 3.30.420.40; -; 2.
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 NCBIfam; TIGR01991; HscA; 1.
DR PANTHER; PTHR19375:SF176; CHAPERONE PROTEIN HSCA; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00679};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00679};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00679}; Reference proteome {ECO:0000313|Proteomes:UP000094070}.
SQ SEQUENCE 616 AA; 66229 MW; 2B87766E1B9FE756 CRC64;
MLLQIAEPGQ SAAPHQHKFA VGIDLGTTNS LVAAVRSGSC TPLVDENEKA ILPSVVHYSS
ETILVGHEAK LRAQQDPKNT ISSVKRLIGR SLLDVQSRYS DLPYQFKASD NGLPLIEVPT
GQVNPIQVSS EILKSLAERA EKTLDHELEG VVITVPAYFD DAQRAGTKDA AELAGLKVLR
LLNEPTAAAI AYGLDSGQEG VIAVYDLGGG TFDISLLRLS KGVFEVLATG GDSALGGDDF
DDLLLDYFKQ QVGIAEKLGA EQHRVLLDAA TQAKIQLSDA DSVNVEVLDK TIVFTRAQFD
QLIQPLVKKT LLSCRRALKD AGVNSDEVAE VVMVGGSTRT PFVRTMVGEF FGRTPLTSIN
PDEVVAIGAG IQADILIGNK PDSDMLLLDV IPLSLGIETM GGLVEKIIPR NTTIPVAKAQ
EFTTFKDGQT AMLVHVAQGE REMIDDCRSL ARFTLNGIPP MKAGAAHIRV TYQVDADGLL
SVTAMEKSTG VQSDIQVKPS YGLSDTEIAD MLRASMTHAK EDMQARALAE QKVEADRVIE
GLLVALQENG EELLSVTEYQ SIEASLKTLI QLRNGDDADA IEQGIKETDK LSQEFASRRM
DVSIRAALSG QSVDDI
//
