ID R8ATL5_PLESH Unreviewed; 617 AA.
AC R8ATL5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 08-NOV-2023, entry version 50.
DE RecName: Full=Chaperone protein HscA {ECO:0000256|ARBA:ARBA00018474, ECO:0000256|HAMAP-Rule:MF_00679};
DE AltName: Full=Hsc66 {ECO:0000256|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000256|HAMAP-Rule:MF_00679,
GN ECO:0000313|EMBL:EON89694.1};
GN ORFNames=PLESHI_04022 {ECO:0000313|EMBL:EON89694.1};
OS Plesiomonas shigelloides 302-73.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Plesiomonas.
OX NCBI_TaxID=1315976 {ECO:0000313|EMBL:EON89694.1, ECO:0000313|Proteomes:UP000014012};
RN [1] {ECO:0000313|EMBL:EON89694.1, ECO:0000313|Proteomes:UP000014012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=302-73 {ECO:0000313|EMBL:EON89694.1,
RC ECO:0000313|Proteomes:UP000014012};
RX PubMed=23814109;
RA Pique N., Aquilini E., Alioto T., Minana-Galbis D., Tomas J.M.;
RT "Genome Sequence of Plesiomonas shigelloides Strain 302-73 (Serotype O1).";
RL Genome Announc. 1:e00404-13(2013).
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. Involved in the maturation of IscU.
CC {ECO:0000256|ARBA:ARBA00025329, 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:EON89694.1}.
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DR EMBL; AQQO01000028; EON89694.1; -; Genomic_DNA.
DR RefSeq; WP_010862433.1; NZ_KB944507.1.
DR AlphaFoldDB; R8ATL5; -.
DR STRING; 703.SAMEA2665130_00568; -.
DR PATRIC; fig|1315976.3.peg.785; -.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000014012; 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:UP000014012}.
SQ SEQUENCE 617 AA; 65557 MW; 9E8027A566F6E98C CRC64;
MALLQIAEPG QMAAPHQHRL AAGIDLGTTN SLVASVRSGQ AQTLPDAEGR HLLPSVVHYG
AGEQGLSVGW DARANAARDP ANTIISVKRL MGRSLADIQA RYPSLPYQFE ASANGLPQIR
TVQGEVNPVQ VSAEILKALS ARAEATLGGP LSGVVITVPA YFDDAQRQGT KDAARLAGLH
VLRLLNEPTA AAIAYGLDSG QEGVIAVYDL GGGTFDISVL RLSRGVFEVL ATGGDSALGG
DDFDHLLADW LAEQAGICTP DSQLQRQLLD EAIRAKIALS DAESVSVQIA NWQGHVSREQ
FASLIRPLVK KTLLACRRAL KDAGISAEEV LEVVMVGGST RTPLVREMVG EFFHRQPLTS
IDPDKVVAIG AGIQADILAG NKPDAEMLLL DVIPLSLGIE TMGGLVEKII PRNTTIPVAR
AQEFTTFKDG QSAMMVHVVQ GERELVDDCR SLARFTLRGI PAMPAGGAHI RVTYQVDADG
LLSVTAMEKS TGVQSSIQVK PSYGLTDDEI VGMLRDSMAN AEQDMQARML AEQQVEADRV
AESLSVALEK DAALLSAAEL ATIEQALGAL RTARQGDRAA DIEAAIKAVD AATQEFAARR
MDESIRRALT GHSVDEM
//
