ID A0A1H0QVY3_9PSED Unreviewed; 621 AA.
AC A0A1H0QVY3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000256|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000256|HAMAP-Rule:MF_00679};
GN ORFNames=SAMN05216193_12550 {ECO:0000313|EMBL:SDP21390.1};
OS Pseudomonas jinjuensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=198616 {ECO:0000313|EMBL:SDP21390.1, ECO:0000313|Proteomes:UP000242957};
RN [1] {ECO:0000313|Proteomes:UP000242957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 21621 {ECO:0000313|Proteomes:UP000242957};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNIJ01000025; SDP21390.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0QVY3; -.
DR STRING; 198616.SAMN05216193_12550; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000242957; 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}; Reference proteome {ECO:0000313|Proteomes:UP000242957}.
SQ SEQUENCE 621 AA; 66437 MW; B2CF1C6610BC17DF CRC64;
MALLQIAEPG QSPQPHQRRL AVGIDLGTTN SLVAAVRSGV AEPLPDEQGR VILPSAVRYL
ADHVEVGDAV KQNAAEDPLN SIISVKRLMG RGLEDVKQLG GQLPYRFSQG ESHMPFIETV
QGAKSPVEVS AEILRTLRQR AEQTLGGDLV GAVITVPAYF DDAQRQATKD AARLAGLHVL
RLLNEPTAAA VAYGLDNNAE GVVAIYDLGG GTFDISILRL TRGVFEVLAT GGDTALGGDD
FDHAIAGWII QQAGLSDDLD PGAQRQLLQV ACAAKEALTD AAQVDVTHAG WTGELTREAF
EALIEPMVAR SLKTCRRALR DSAVEQEEVT AVVMVGGSTR VPRVRQAVGE LFGLTPLTDI
DPDQVVAIGA AIQADTLAGN KRGDGEELLL LDVIPLSLGL ETMGGLMEKV IPRNTTIPVA
RAQDFTTYKD GQTAMMIHVL QGERELVKDC RSLARFELRG IPPMVAGAAK IRVSFQVDAD
GLLGVSAREL GSGVEASIQV KPSYGLTDGE IARMLQDSFQ YAGDDMAARA LREQQVEAER
LLEAVQSALD ADGERLLDAE EREVIDANMQ TLRELAAGND TAAIEMQIKR LSQVTDAFAA
RRMDATVKAA LAGRRLNEIE E
//
