HSCA_METCA
ID HSCA_METCA Reviewed; 619 AA.
AC Q60C59;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=MCA0252;
OS Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylococcus.
OX NCBI_TaxID=243233;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J.,
RA Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L.,
RA Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H.,
RA Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R.,
RA Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.;
RT "Genomic insights into methanotrophy: the complete genome sequence of
RT Methylococcus capsulatus (Bath).";
RL PLoS Biol. 2:1616-1628(2004).
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; AE017282; AAU90590.1; -; Genomic_DNA.
DR AlphaFoldDB; Q60C59; -.
DR SMR; Q60C59; -.
DR STRING; 243233.MCA0252; -.
DR EnsemblBacteria; AAU90590; AAU90590; MCA0252.
DR KEGG; mca:MCA0252; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_6; -.
DR OMA; PDPHQRR; -.
DR Proteomes; UP000006821; 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..619
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_0000078632"
SQ SEQUENCE 619 AA; 65948 MW; 4FBE4637C33AE6EF CRC64;
MLLQISEPGA GVKPQRRLAV GIDLGTTHSL VATVRDEQTV VLGDAQGRVL LPSVVRYLGA
GAIEVGYEAK ARQAEDPENT FVSVKRYMGR GLGDLASHHG APYRFVEGEG MVQFDTRAGR
ISPVQVSAEI LKVLRDRAVA ELGGELAGAV ITVPAYFDEA QRQATKDAAK LAGLEVFRLL
NEPTAAAVAY GLDNAAEGVY AVYDLGGGTF DISVLKLTRG VFEVLATNGD PALGGDDFDR
AVYDWLLAQS GLNGLSSSDA SLLLTASRAA KERLSEQTEA TVDTMLSDGS RIVATLSRDT
FAELTAGLVK KTLTPVRKAL RDAGLAIDDI KGVVLVGGAT RMPCIREAVA EFFQQTPLTD
LDPDKVVALG AAMQANLLAG NRAGGDWLLL DVIPLSLGIE TLGGLCEKIV PRNTTIPVAR
AQEFTTWKDG QTAMSIHVVQ GERELVSECR SLARFELRGI PPMAAGAARI RVTYQVDADG
LLNVTAAEQT SGVEARIEVK PSYGLSDAEV ARMIEDSYLH ARDDLEARRL QEQKVEAARL
IEATESALTE DGGLLTEQEL EVLVKGLQVL KGAMEGSDWQ AIKNAADALN EASTEFAGRR
MDHSIKAALT GQKLESLGV