ID G4A5T1_AGGAC Unreviewed; 619 AA.
AC G4A5T1;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000256|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000256|HAMAP-Rule:MF_00679};
GN ORFNames=SC1083_0166 {ECO:0000313|EMBL:EGY35166.1};
OS Aggregatibacter actinomycetemcomitans serotype e str. SC1083.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Aggregatibacter.
OX NCBI_TaxID=907488 {ECO:0000313|EMBL:EGY35166.1, ECO:0000313|Proteomes:UP000005508};
RN [1] {ECO:0000313|EMBL:EGY35166.1, ECO:0000313|Proteomes:UP000005508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC1083 {ECO:0000313|EMBL:EGY35166.1,
RC ECO:0000313|Proteomes:UP000005508};
RA Chen C., Kittichotirat W., Asikainen S., Bumgarner R.;
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00679}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|HAMAP-Rule:MF_00679,
CC ECO:0000256|RuleBase:RU003322}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGY35166.1}.
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DR EMBL; AEJM01000003; EGY35166.1; -; Genomic_DNA.
DR RefSeq; WP_005555595.1; NZ_AEJM01000003.1.
DR AlphaFoldDB; G4A5T1; -.
DR SMR; G4A5T1; -.
DR PATRIC; fig|907488.3.peg.163; -.
DR Proteomes; UP000005508; Unassembled WGS sequence.
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; 3.30.420.40; -; 2.
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 NCBIfam; TIGR01991; HscA; 1.
DR PANTHER; PTHR19375:SF176; CHAPERONE PROTEIN HSCA; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00679};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00679};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00679}.
SQ SEQUENCE 619 AA; 66869 MW; 23A932FAC9079521 CRC64;
MALLQIAEPG QSAAPHQHKL AVGIDLGTTN SLIASVRNGH SEILLDGQDR PLLPSIVHFG
GDDNIIVGYE AAELAAQDPQ NTVISVKRLI GRSLADIQQR YPNLPYQFVA SENGLPLLQT
TQGARSPIEV SAEILKKLTA LGEQRLGGSL VGAVITVPAY FDDAQRQSTK DAAKLAGLNV
LRLLNEPTAA AIAYGLDSGQ EGVIAVYDLG GGTFDISILR LSRGVFEVLA TGGDTALGGD
DFDLLLANWI IEQSAVKPEN DNQYRELIEL ANQIKLTLSH ETETQIHYRN WLGNITREQF
NELIQPLVKR SLLACRRALK DAGVEADDVH EVVMVGGSTR VPYVREQVGE FFQKQPLTSI
DPDKVVALGA AIQADTLAGN KPDSDLLLLD VIPLSLGIET MGGLVEKIIP RNTTIPVARA
QEFTTFKDGQ TAMSVHIVQG EREMVADCRS LARFTLRGIP PMAAGAAHIR VTYQVDADGL
LSVTAMEKAT GVQSSIQVKP SYGLTDDEIA NMLKASMENA KEDIQARLLA EQRVEAERVL
ESVRSALAQD YDLLDDDELS AVKNAIISLE QLKQQEDSIA IKQGIKALDL ATQDFAARRM
DKSIRAALAG QSVEDIVGK
//
