HSCA_ALISL
ID HSCA_ALISL Reviewed; 617 AA.
AC B6EGX9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=VSAL_I0721;
OS Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS LFI1238)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=316275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LFI1238;
RX PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT LFI1238 shows extensive evidence of gene decay.";
RL BMC Genomics 9:616-616(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}.
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DR EMBL; FM178379; CAQ78406.1; -; Genomic_DNA.
DR RefSeq; WP_012549526.1; NC_011312.1.
DR AlphaFoldDB; B6EGX9; -.
DR SMR; B6EGX9; -.
DR STRING; 316275.VSAL_I0721; -.
DR EnsemblBacteria; CAQ78406; CAQ78406; VSAL_I0721.
DR KEGG; vsa:VSAL_I0721; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; PDPHQRR; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001730; Chromosome 1.
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_1000131664"
SQ SEQUENCE 617 AA; 65872 MW; 679BEF83A902061E CRC64;
MAFLQISEPG QSAAPHQHKL AVGIDLGTTN SLVASVRSGE ANTLPDMKGN VILPSVVQYQ
DDKICVGANA YQSAASDPQN TIISVKRLMG RSLKDIQTRY PDLPYQFTES DNGLPVIHTT
QGDVNPIQVS AEILKSLSNR AEVTLGGSLE GVVITVPAYF DDAQRAGTKD AATLAGLNVL
RLLNEPTAAA IAYGLDSGQE GIIAVYDLGG GTFDISILRL SKGVFEVLAT GGDSALGGDD
FDHVLSQWIK DQAEITTALS NQEQRELLTL ATETKVALSD ADSVTVSFKE WSGTITADIF
NQLIQSLVKK TLMACRRALK DADISSEDVM EVVMVGGSTR TPIVRRSVGD YFAKTPLTSI
DPDQVVAIGA AIQADILVGN KPDTEMLLLD VIPLSLGIET MGGLVEKIIP RNTTIPVAKA
QEFTTFKDGQ TGMMVHVVQG EREMVEDGRS LARFSLKGIP PMTAGAAHIR VTYQVDADGL
LSVTAMEKST GVQSHIQVKP SYGLSDNEVA TMLKDSMTYA KDDMKARALA EQQVEADRVI
EGLVVALNND GDALLSKEEQ TVILQAVEAL ITVRKGTDTQ AIEDGIKHAD EASQEFAARR
MDASIRAALA GQSIDEV
