HSCA_ACTSZ
ID HSCA_ACTSZ Reviewed; 614 AA.
AC A6VMP1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Asuc_0868;
OS Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS 130Z).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=339671;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z;
RX PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA Burkhart K.B., Harkins V., Vieille C.;
RT "A genomic perspective on the potential of Actinobacillus succinogenes for
RT industrial succinate production.";
RL BMC Genomics 11:680-680(2010).
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; CP000746; ABR74238.1; -; Genomic_DNA.
DR RefSeq; WP_012072616.1; NC_009655.1.
DR AlphaFoldDB; A6VMP1; -.
DR SMR; A6VMP1; -.
DR STRING; 339671.Asuc_0868; -.
DR EnsemblBacteria; ABR74238; ABR74238; Asuc_0868.
DR KEGG; asu:Asuc_0868; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_3_6; -.
DR OMA; PDPHQRR; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001114; 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..614
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_1000072728"
SQ SEQUENCE 614 AA; 66225 MW; 1D4F282B52F2C370 CRC64;
MALLQIAEPG QSAAPHQHKL AIGIDLGTTN SLVATVRNGQ AEILLDEKER PLTPSIVHYG
DNVTVGYDAG ELASRDPQNT IISVKRLIGR SLNDVQARYP NLPYRFVRSE NGLPLLGTAQ
GNVSPIEVSG EILKKLTALA QHRLNGELLG VVITVPAYFD DAQRQSTKDA AKLAGLNVLR
LLNEPTAAAI AYGLDSGREG VIAVYDLGGG TFDISILRLS RGVFEVLATG GDTALGGDDF
DHLIADWISE KSGIQPQDDQ QKRLLIELAA RTKIALTDKP QVSLSYQGWQ GEMQREEFNG
LISGLVKRSL MACRRALKDA GIGQSEVQEV VMVGGSTRVP FVRDQVGEFF QRRPLTSIDP
DKVVALGAAI QADILVGNKP DNEMLLLDVI PLSLGIETMG GLVEKIIPRN TTIPVARAQE
FTTFKDGQTA MSVHVVQGER ELVGDCRSLA RFTLRGIPPM AAGAAHIRVT YQVDADGLLS
VTAMEKSTGV QSSIQVKPSY GLTDDEITQM LKASMENAKE DIGARMLAEQ RVEARRVIEA
VLSALLDDQD LLNDEELSTV KNALVSLDNL QQGTDTQAIK AGIKALDAAT QEFAARRMDK
SIRRALSGQS VDSL
