HSCA_AERS4
ID HSCA_AERS4 Reviewed; 615 AA.
AC A4SP09;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=ASA_2607;
OS Aeromonas salmonicida (strain A449).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=382245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A449;
RX PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA Brown L.L.;
RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT the evolution of a fish pathogen.";
RL BMC Genomics 9:427-427(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}.
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; CP000644; ABO90631.1; -; Genomic_DNA.
DR RefSeq; WP_005310412.1; NC_009348.1.
DR AlphaFoldDB; A4SP09; -.
DR SMR; A4SP09; -.
DR STRING; 382245.ASA_2607; -.
DR EnsemblBacteria; ABO90631; ABO90631; ASA_2607.
DR KEGG; asa:ASA_2607; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_6; -.
DR OMA; PDPHQRR; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000225; 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.
FT CHAIN 1..615
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_1000044841"
SQ SEQUENCE 615 AA; 65216 MW; F8F502C3C34A5FF2 CRC64;
MALLQIAEPG QSAAPHQHKR AVGIDLGTTN SLVAAVRSGH ADTLCDEQGR DLLPSVVHYQ
VDAIRVGFDA KREASLDPHN TIVSAKRMMG KALADIDTRQ QPYEFVAADN GMPQLQTRQG
LVNPVQVSAE ILKKLAERGA AALGGELDGV VITVPAYFDD AQRQGTKDAA RLAGLHVLRL
LNEPTAAAIA YGLDSGQEGV IAVYDLGGGT FDISILRLHR GVFEVMATGG DSALGGDDFD
HLLADWIKAQ AGLEGQLDAS TQRELLDVAA AVKHGLTDAD LVPCAFAGWQ GEVSRHLFEE
LITPLVKRTL LACRRALRDA GLEQVEVLEV VMVGGSTRVP LVRERVGEFF QRTPLTSIDP
DKVVAIGAAI QADILVGNKP DAEMLLLDVI PLSLGLETMG GLAEKVIPRN TTIPVARAQE
FTTFKDGQTA MAIHVVQGER ELVADCRSLA RFTLTGIPPM AAGAAHIRVT FQVDADGLLS
VSAMEKSSGV QAEIQVKPSY GLGEEDILTM LSASIANAQQ DMDARMLAEQ QVEADRVVES
LNAALAADGD ALLSTAERAA IDSAITHVLS VRAAGTTNQI KDAIEAADAV SGEFAARRMD
ASIRKVLTGQ NVNKV
