ID A0A0Q5YX30_9BURK Unreviewed; 619 AA.
AC A0A0Q5YX30;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000256|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000256|HAMAP-Rule:MF_00679};
GN ORFNames=ASG30_09720 {ECO:0000313|EMBL:KQT10129.1};
OS Ramlibacter sp. Leaf400.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=1736365 {ECO:0000313|EMBL:KQT10129.1, ECO:0000313|Proteomes:UP000051173};
RN [1] {ECO:0000313|EMBL:KQT10129.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT10129.1,
RC ECO:0000313|Proteomes:UP000051173};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT10129.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT10129.1,
RC ECO:0000313|Proteomes:UP000051173};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQT10129.1}.
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DR EMBL; LMQL01000011; KQT10129.1; -; Genomic_DNA.
DR RefSeq; WP_055897562.1; NZ_LMQL01000011.1.
DR AlphaFoldDB; A0A0Q5YX30; -.
DR STRING; 1736365.ASG30_09720; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000051173; 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}; Chaperone {ECO:0000256|HAMAP-Rule:MF_00679};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00679}; Reference proteome {ECO:0000313|Proteomes:UP000051173}.
SQ SEQUENCE 619 AA; 66045 MW; 932CBE313C659DAD CRC64;
MALLQISEPG QAPDPHQRRI AVGIDLGTTH SLVASVRNGV AECLPDDQGR VLLPSVVRYL
ENAGRQIGHE AQAAQAHDAE NTIASVKRFM GRGLADIANR ERLPYGFVDQ PGMVSLRTRA
GEKSPVEVSA EILATLRYRA EDTFNDDLYG AVITVPAYFD DAQRQATKDA AQLAGLKVLR
LINEPTAAAI AYGLDNASEG VYAVYDLGGG TFDISILRMS RGVFEVIAAG GDSALGGDDY
DRALAEHLLA KAGVRAATPA DKAAVKVEAR AAKERLTDEE QTEAVLLLSS GEVSVPVTRA
DFERVTADLT QRTLAAVRKA VRDAKLQRDE IQGVVLVGGS TRMPQVRRAV ADFFGREPLI
NLNPDEVVAL GAALQANQLA GNNASGDLLL LDVIPLSLGI ETMGGLVERI VPRNETIPTA
KAQDFTTYQD GQTAMALHVV QGERDLVQDC RSLARFELRG IPPMAAGAAR IRVTFTVDAD
GLLSVNAREQ GSGVEARIDV KPSYGLSDDQ VATMLQESFS TAQQDMKARA VAEARIDAQR
MLLATQSALN ADGGLLDTGE RASVDALMQE LRSVTESSQD AGAIEAATEA LAKGTEDFAA
RRMNRSIRQA LAGRNVETL
//
