HSCA_METPP
ID HSCA_METPP Reviewed; 618 AA.
AC A2SI25;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Mpe_A2258;
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Methylibium.
OX NCBI_TaxID=420662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1;
RX PubMed=17158667; DOI=10.1128/jb.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(2007).
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; CP000555; ABM95214.1; -; Genomic_DNA.
DR RefSeq; WP_011829851.1; NC_008825.1.
DR AlphaFoldDB; A2SI25; -.
DR SMR; A2SI25; -.
DR STRING; 420662.Mpe_A2258; -.
DR PRIDE; A2SI25; -.
DR EnsemblBacteria; ABM95214; ABM95214; Mpe_A2258.
DR KEGG; mpt:Mpe_A2258; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_4; -.
DR OMA; PDPHQRR; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000366; 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..618
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_1000044866"
SQ SEQUENCE 618 AA; 65709 MW; 6E188BA665317E14 CRC64;
MALLQISEPG QSPDPHQRRI AVGIDLGTTH SLVAAVRSGV AECLPDDEGR VILPSAVRYL
EGGRRAIGFD ALAAQAEDPE NTIVSAKRFM GRTLTDIDDR EKLPYRFVDQ PGMVSVATRD
GVKTPVEVSA ELLATLRFRA EDSFDDELFG AVITVPAYFD DAQRQATKDA AQLAGLNVLR
LINEPTAAAI AYGLENGSEG LYAVYDLGGG TFDISLLRLS EGVFEVVATG GDSALGGDDY
DHALADWALA GAGLAAETAQ DKRAVLVAAR AVKEALSSAA EARMQVVLRA GLLDLAVTRV
QFEALTKPLT DRTLAAVRKV LRDAKVSKDE VKGVVLVGGS TRMPQIREAV TLYLGRSPLT
DLNPDEVVAL GAAIQAHQLA GNASGNDLLL LDVTPLSLGL ETMGGLVERI IPRNSSIPTA
RAQDFTTFKD GQTAMAIHVL QGEREQVEYC RSLARFELRG IPPMVAGAAR IRVSFQVDAD
GLLSVTAREQ TSGVEAAVTV KPSYGLADEQ IARMLQEGFT TAEGDMRDRA LREARVETER
MVLATRAALA ADGDLLADGE RAGIEALMRA AEQQALGEDA AAIDAAVKAL ADGTESFAAE
RMNRGIRQAL AGRRVEEV
