ID D2Z887_9BACT Unreviewed; 693 AA.
AC D2Z887;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Patatin {ECO:0000313|EMBL:EFC91684.1};
GN ORFNames=Dpep_1658 {ECO:0000313|EMBL:EFC91684.1};
OS Dethiosulfovibrio peptidovorans DSM 11002.
OC Bacteria; Synergistota; Synergistia; Synergistales;
OC Dethiosulfovibrionaceae; Dethiosulfovibrio.
OX NCBI_TaxID=469381 {ECO:0000313|EMBL:EFC91684.1, ECO:0000313|Proteomes:UP000006427};
RN [1] {ECO:0000313|EMBL:EFC91684.1, ECO:0000313|Proteomes:UP000006427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11002 {ECO:0000313|EMBL:EFC91684.1,
RC ECO:0000313|Proteomes:UP000006427};
RX PubMed=21304695;
RA Labutti K., Mayilraj S., Clum A., Lucas S., Glavina Del Rio T., Nolan M.,
RA Tice H., Cheng J.F., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Goodwin L., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Spring S., Goker M.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Permanent draft genome sequence of Dethiosulfovibrio peptidovorans type
RT strain (SEBR 4207).";
RL Stand. Genomic Sci. 3:85-92(2010).
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:EFC91684.1}.
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DR EMBL; ABTR02000001; EFC91684.1; -; Genomic_DNA.
DR RefSeq; WP_005661228.1; NZ_ABTR02000001.1.
DR AlphaFoldDB; D2Z887; -.
DR STRING; 469381.Dpep_1658; -.
DR PaxDb; 469381-Dpep_1658; -.
DR eggNOG; COG1752; Bacteria.
DR OrthoDB; 9770965at2; -.
DR Proteomes; UP000006427; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd07205; Pat_PNPLA6_PNPLA7_NTE1_like; 1.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002641; PNPLA_dom.
DR PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR PANTHER; PTHR14226:SF82; PATATIN-LIKE PROTEIN, PLPD; 1.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS51635; PNPLA; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000006427};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..693
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003040439"
FT DOMAIN 31..220
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
SQ SEQUENCE 693 AA; 75526 MW; 51418ACBDF2E1C69 CRC64;
MKKKRLALFL AMCFCFSMSS SSMAKTGAIV LALSGGGTKG LAHVGVLKAL KAEGIPIAGI
VGTSMGAIIG GLSAAGYSPQ ELEDVLEKVD IGGIILGNGE NRNSEPKNRE ISPLMPKLEL
NAHGQVIGPK GPLSGATALN LFQKLTSRVS VVQFNELPIP FAAVATDLET GEKVVLRHGS
LASAMRASMS IPGLFEPWPI EGRLLVDGGL VSNMPVTTAK EMFPDYPIVA VNVCSDLRKS
DEMKTMVDVI DQTITILTSQ NVDREESKAD VIIKPKVGNM ATLGNVEIRD MVRLGVVAAE
DKMAAIKSLA VRAPSAPEHR PTILRLVRRI SVEGVPEDFA DNIKGKFSDW IGRPVHPEDI
VSAAEWIRSR EDVKTVDYQL VEKIDGVDVL LKIQRQPAYR IALDGHATNL SGGSWIGIRS
RMMDLAYDGD YLNVDAILGD DWAAKADYHF AVDKGSYEMG LRAGRVSMKP RGKWDMLSLS
IGRTFGTDGS SLTIGALGSK MEGSGQTVEA WGPIVKWYSS GIKGQDAPED ESYLSFGAWY
PSEGEEMLFR IEGGVDKPLS SRWRGYLKAG LMEGNSDGRY IGQGAYLGAR EELYSLADRP
ILGERFAWWR LGFRRRLGES GDSLWEGELF GGQGYVWDNG GDLFDEPWEV GVALTVPSRL
LKARFLAIYD DDNDWTFGFS IGDPMWTLRY PFP
//
