ID K6XTX6_9ALTE Unreviewed; 621 AA.
AC K6XTX6;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000256|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000256|HAMAP-Rule:MF_00679,
GN ECO:0000313|EMBL:GAC15141.1};
GN ORFNames=GLIP_2515 {ECO:0000313|EMBL:GAC15141.1};
OS Aliiglaciecola lipolytica E3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Aliiglaciecola.
OX NCBI_TaxID=1127673 {ECO:0000313|EMBL:GAC15141.1, ECO:0000313|Proteomes:UP000006334};
RN [1] {ECO:0000313|EMBL:GAC15141.1, ECO:0000313|Proteomes:UP000006334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E3 {ECO:0000313|EMBL:GAC15141.1,
RC ECO:0000313|Proteomes:UP000006334};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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:GAC15141.1}.
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DR EMBL; BAEN01000049; GAC15141.1; -; Genomic_DNA.
DR RefSeq; WP_008844946.1; NZ_BAEN01000049.1.
DR AlphaFoldDB; K6XTX6; -.
DR STRING; 1127673.GLIP_2515; -.
DR eggNOG; COG0443; Bacteria.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000006334; 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.
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:UP000006334}.
SQ SEQUENCE 621 AA; 66741 MW; 0D9EB95D54253AAF CRC64;
MALLQIAEPG QAAAPHQRKL AVGIDLGTTN SLVATVRSGK PETLPDQFGR HILPSVVQYS
SSETIVGEQA KQSANLDPAN TIVSVKRLMG RSLKDIQTHY PNLPYEFVTD KEQITIKVPG
STVNPIQVSA EILANLKARA EDSLGDELTG AVVTVPAYFD DAQRQGTKDA AQLAGLHVLR
LLNEPTAAAI AYGLDSGQEG VIAIYDLGGG TFDISILRLS KGVFEVLATG GDTALGGDDF
DQLLFDYICK QANLPAEISK GLRRRLLDDA KLAKEALSND SAVDIQFTDD QGDSHEVVIS
CLTFESLIEP LVKKSLRACR RAVKDAEVEL EDVLQVVMVG GSTRVPMVRH KVGEFFGKTP
LTSIDPDKVV AIGAAIQADI LAGNKPDNEM LLLDVLPLSL GIETMGGLTE KIVARNTTIP
VAKAQEFTTF KDGQTAMMVH VLQGERELVK DCRSLAKFNL TGIPPMAAGA AHIRVTFQVD
ADGLLNVTAM EKSTGVKAEI QVKPSYGLED AEVAEMLKSS MLHAKQDMQA RMLKEQQVEA
SRVAETLNSA LQKDGDELLS KDENAAIKDA LQQMLSLAEG TDIEAIKTAI EKVDNISQAF
AARRMDKSIN QALTGHSVNE I
//
