ID F3G3G2_PSESJ Unreviewed; 564 AA.
AC F3G3G2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Heat shock protein Hsp70 {ECO:0000313|EMBL:EGH41612.1};
GN ORFNames=PSYPI_03944 {ECO:0000313|EMBL:EGH41612.1};
OS Pseudomonas syringae pv. pisi str. 1704B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=629263 {ECO:0000313|EMBL:EGH41612.1, ECO:0000313|Proteomes:UP000004986};
RN [1] {ECO:0000313|EMBL:EGH41612.1, ECO:0000313|Proteomes:UP000004986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1704B {ECO:0000313|EMBL:EGH41612.1,
RC ECO:0000313|Proteomes:UP000004986};
RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT genomics of 19 Pseudomonas syringae isolates.";
RL PLoS Pathog. 7:E1002132-e1002132(2011).
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, 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:EGH41612.1}.
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DR EMBL; AEAI01000182; EGH41612.1; -; Genomic_DNA.
DR AlphaFoldDB; F3G3G2; -.
DR PATRIC; fig|629263.4.peg.656; -.
DR HOGENOM; CLU_005965_2_4_6; -.
DR BioCyc; PSYR629263:G11X0-922-MONOMER; -.
DR Proteomes; UP000004986; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR CDD; cd10235; HscC_like_NBD; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR042030; HscC_NBD.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
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|RuleBase:RU003322};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Stress response {ECO:0000313|EMBL:EGH41612.1}.
SQ SEQUENCE 564 AA; 62869 MW; 908B656F2BA52E29 CRC64;
MIVDIDLGTT NSLVAVWRDG SSELVTNALG ETLTPSVVGL DDDGQILVGK AARERLQTHP
EKTTALFKRY MGSAQEIRLG SATYRPEELS SLVLKSLKAD VERAFGEPVT EAVISVPAYF
SDAQRKATRI AGELAGLKVE KLINEPTAAA LAYGLHQKEG ETSFLVFDLG GGTFDISILE
LFDGVMEVRA SAGDNFLGGE DFDQVMVEHF VNLHRDEPDF PSTELIAPAL RREAERVRRA
LGQDGSADFV LRHADREWRK TITQEQMSDF YAPLLNRLRA PAERALRDAR IRVADLDEIL
LVGGTTRMPL IRKLAASLFG RFPSIALNPD EIVAQGAAVQ AALKHRDAAL EEIVLTDVCP
YTLGIETITQ VGNRYESGHY LPIIERNSVV PVSRVKTVQT VSDDQEHVMV RIFQGESRMV
KDNIALGELI IPIPRAKAGE VALDVRFTYD NNGLLEADVM TQLTGERHKL VIENNPGVMT
PDEIQERLQV LEALKVHPRD QQANTHLIAR LERLYQECLG SDRELIDHWT TQFQHVLETQ
DERQISEIRK QLKQEVDTFE QGAR
//
