HSCA_AERHH
ID HSCA_AERHH Reviewed; 615 AA.
AC A0KJ36;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=AHA_1751;
OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=380703;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC
RC 2358 / NCIMB 9240 / NCTC 8049;
RX PubMed=16980456; DOI=10.1128/jb.00621-06;
RA Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H.,
RA Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL J. Bacteriol. 188:8272-8282(2006).
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; CP000462; ABK37680.1; -; Genomic_DNA.
DR RefSeq; WP_011705638.1; NC_008570.1.
DR RefSeq; YP_856287.1; NC_008570.1.
DR AlphaFoldDB; A0KJ36; -.
DR SMR; A0KJ36; -.
DR STRING; 380703.AHA_1751; -.
DR EnsemblBacteria; ABK37680; ABK37680; AHA_1751.
DR KEGG; aha:AHA_1751; -.
DR PATRIC; fig|380703.7.peg.1765; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; PDPHQRR; -.
DR Proteomes; UP000000756; Chromosome.
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.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding; Reference proteome.
FT CHAIN 1..615
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_1000044840"
SQ SEQUENCE 615 AA; 65304 MW; 46DCBB32A9362B15 CRC64;
MALLQIAEPG QSAAPHQHKR AVGIDLGTTN SLVAAVRSGQ ADTLCDEQGR DLLPSVVHYQ
ADTIRVGVDA KREAALDPHN TIVSAKRMMG KALADIDTRQ QPYQFVAADN GMPQLQTRQG
LVNPVQVSAE ILKKLAERGA AALGGDLDGV VITVPAYFDD AQRQGTKDAA RLAGLHVLRL
LNEPTAAAIA YGLDSGQEGV IAVYDLGGGT FDISILRLHR GVFEVMATGG DSALGGDDFD
HLLADWLKEQ AGLTGELDAR LQRELLDVAA AVKHGLTDAD AVPCTFAGWQ GSVTRSQFDE
LIQPLVKRTL LACRRALRDA GLEQEEVLEV VMVGGSTRVP LVRELVGEFF QRPPLTSIDP
DKVVAIGAAI QADILVGNKP DAEMLLLDVI PLSLGLETMG GLAEKVIPRN TTIPVARAQE
FTTFKDGQTA MAIHVVQGER ELVADCRSLA RFTLTGIPPM VAGAAHIRVT FQVDADGLLS
VSAMEKSSGV QAEIQVKPSY GLGEDDILNM LSASIANAQQ DMDARMLAEQ QVEADRVVES
LNAALAADGE ALLSPAERAE LDAAIAHLLT MRSTGTTNQI KEAIEAADAA SGEFAARRMD
ASIRKVLTGQ NVNKV