ID A0A2D0KMC4_9GAMM Unreviewed; 615 AA.
AC A0A2D0KMC4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 34.
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 ORFNames=Xsto_02944 {ECO:0000313|EMBL:PHM64538.1};
OS Xenorhabdus stockiae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351614 {ECO:0000313|EMBL:PHM64538.1, ECO:0000313|Proteomes:UP000222366};
RN [1] {ECO:0000313|EMBL:PHM64538.1, ECO:0000313|Proteomes:UP000222366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17904 {ECO:0000313|EMBL:PHM64538.1,
RC ECO:0000313|Proteomes:UP000222366};
RX PubMed=28993611; DOI=10.1038/s41564-017-0039-9;
RA Tobias N.J., Wolff H., Djahanschiri B., Grundmann F., Kronenwerth M.,
RA Shi Y.M., Simonyi S., Grun P., Shapiro-Ilan D., Pidot S.J., Stinear T.P.,
RA Ebersberger I., Bode H.B.;
RT "Natural product diversity associated with the nematode symbionts
RT Photorhabdus and Xenorhabdus.";
RL Nat. Microbiol. 2:1676-1685(2017).
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:PHM64538.1}.
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DR EMBL; NJAJ01000028; PHM64538.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2D0KMC4; -.
DR Proteomes; UP000222366; 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 615 AA; 66166 MW; 1A907D88AA1FFB27 CRC64;
MALLQISEPG LSAAPHQRRL AAGIDLGTTH SLVATVRSGQ AETLADSENR HLLPSVVQYC
KDEIQIGWQA RQQAAFDPVN TISSVKRMMG RSLADIQQRY PNLPYQFQAS ENGLPLINTA
AGLVDPIQVS SDILKSLAQR AEETLDGKLD GVVITVPAYF DDAQRQGTKD AARLAGLHVL
RLLNEPTAAA IAYGLDSGQE GVIAVYDLGG GTFDVSILRL SRGVFEVLAT GGDTALGGDD
FDHLLADWIR EQAGITDTDH GLQRQLLDVA TQTKIALSDE DSVSINFADW QGNITRTEFN
ELITTLVKRT LLACRRALKD AGVTADEVLQ VVMVGGSTRV PLVRSMVGEF FDREPLTSID
PDKVVAVGAA IQADILAGNK PDSEMLLLDV IPLSLGLETM GGLVEKVIPR NTTIPVARAQ
EFTTFKDGQS AMSIHVVQGE RELVTDCRSL ARFTLRGIPP LPAGGAHIRV TFQVDADGLL
SVSALEKSTG VEASIQVKPS YGLSDEEIAR MIKDSMSNAQ EDIQARKLAE QKVEAARVLE
SLTGALEKDA DLLSQEEHTA IDAAVQVLIE SAQGTSPEAI ESAIKQLDKQ TQEFAARRMD
TSIRRALAGH SVDEI
//
