ID A0A0Q8ETV6_9GAMM Unreviewed; 565 AA.
AC A0A0Q8ETV6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=2-alkenal reductase {ECO:0000313|EMBL:KRA44385.1};
GN ORFNames=ASD72_10275 {ECO:0000313|EMBL:KRA44385.1};
OS Pseudoxanthomonas sp. Root630.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1736574 {ECO:0000313|EMBL:KRA44385.1, ECO:0000313|Proteomes:UP000051081};
RN [1] {ECO:0000313|EMBL:KRA44385.1, ECO:0000313|Proteomes:UP000051081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root630 {ECO:0000313|EMBL:KRA44385.1,
RC ECO:0000313|Proteomes:UP000051081};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA44385.1, ECO:0000313|Proteomes:UP000051081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root630 {ECO:0000313|EMBL:KRA44385.1,
RC ECO:0000313|Proteomes:UP000051081};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KRA44385.1}.
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DR EMBL; LMGY01000016; KRA44385.1; -; Genomic_DNA.
DR RefSeq; WP_056880478.1; NZ_LMGY01000016.1.
DR AlphaFoldDB; A0A0Q8ETV6; -.
DR STRING; 1736574.ASD72_10275; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000051081; 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:SF439; CHAPERONE PROTEIN HSCC; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR Pfam; PF00012; HSP70; 2.
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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322}.
SQ SEQUENCE 565 AA; 61518 MW; 15A46E088482128D CRC64;
MIVGIDLGTT HSLVGVYEDG APRLIPNALG KLLTPSVVSV GEDGTILVGD AARDRLISHP
QASVASFKRW MGSRRETRLG QRAYLPEELS ALVIRSLLDD AEVALGHRPQ EAVISVPAYF
SDAQRRATRR AGELAGVRVE RLINEPTAAA LAYGLAQKLD DAHVLVLDLG GGTFDVSILE
LFDGVVKVHA SAGDNYLGGD DFTEAIEKHW LSENELRGEA LKPHEASQLR QRAEAAKRTL
AMGQPAEVAL YVDGKLYSLS LDESGFEQIV APLVTRMRSP IERAMRDAGL RGGDLAEVVM
VGGASRMQQL SKLAARLLGR LPLRHVAPDE AIAHGACVAA GLKARDETLE EIILTDVCPH
SLGVAVSMEL GQGMRSHGHF DPIIERNCTV PVSRVREYFP VHDQQNAITL RVYQGENPWA
ENNIALGELE VPVPPGATQE RGVDVRFTYD INGVLQVEAR VQKTGIVREL LLMQGDGGLS
EEEARKRLAE LAGLKTHPRD EQPNIAALAR AERLYVESLG DERRHVQGLI VEFQAALATQ
DKAFVARQRD ALLQALDQYE TRGPL
//