ID A0A6V8LXM1_9BACT Unreviewed; 634 AA.
AC A0A6V8LXM1;
DT 10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2021, sequence version 1.
DT 02-APR-2025, entry version 13.
DE SubName: Full=Lipase 1 {ECO:0000313|EMBL:GFK95331.1};
DE EC=3.1.1.3 {ECO:0000313|EMBL:GFK95331.1};
GN Name=lip-1 {ECO:0000313|EMBL:GFK95331.1};
GN ORFNames=NNJEOMEG_03190 {ECO:0000313|EMBL:GFK95331.1};
OS Fundidesulfovibrio magnetotacticus.
OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfovibrionia;
OC Desulfovibrionales; Desulfovibrionaceae; Fundidesulfovibrio.
OX NCBI_TaxID=2730080 {ECO:0000313|EMBL:GFK95331.1, ECO:0000313|Proteomes:UP000494245};
RN [1] {ECO:0000313|EMBL:GFK95331.1, ECO:0000313|Proteomes:UP000494245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SIID29052-01 {ECO:0000313|EMBL:GFK95331.1,
RC ECO:0000313|Proteomes:UP000494245};
RG Desulfovibrio sp. FSS-1 genome sequencing consortium;
RA Shimoshige H., Kobayashi H., Maekawa T.;
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GFK95331.1, ECO:0000313|Proteomes:UP000494245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SIID29052-01 {ECO:0000313|EMBL:GFK95331.1,
RC ECO:0000313|Proteomes:UP000494245};
RA Shimoshige H., Kobayashi H., Maekawa T.;
RT "Draft genome sequence of Desulfovibrio sp. strainFSS-1.";
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000256|ARBA:ARBA00008668}.
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:GFK95331.1}.
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DR EMBL; BLTE01000016; GFK95331.1; -; Genomic_DNA.
DR RefSeq; WP_173086251.1; NZ_BLTE01000016.1.
DR AlphaFoldDB; A0A6V8LXM1; -.
DR Proteomes; UP000494245; Unassembled WGS sequence.
DR GO; GO:0019867; C:outer membrane; IEA:InterPro.
DR GO; GO:0004806; F:triacylglycerol lipase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.40.128.130; Autotransporter beta-domain; 1.
DR Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR InterPro; IPR005546; Autotransporte_beta.
DR InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR InterPro; IPR017186; Lipase_autotranspt_EstA.
DR InterPro; IPR006315; OM_autotransptr_brl_dom.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR NCBIfam; TIGR01414; autotrans_barl; 1.
DR Pfam; PF03797; Autotransporter; 1.
DR PIRSF; PIRSF037375; Autotrns_EstA; 1.
DR SMART; SM00869; Autotransporter; 1.
DR SUPFAM; SSF103515; Autotransporter; 1.
DR PROSITE; PS51208; AUTOTRANSPORTER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:GFK95331.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000494245};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..634
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5029002313"
FT DOMAIN 357..634
FT /note="Autotransporter"
FT /evidence="ECO:0000259|PROSITE:PS51208"
FT ACT_SITE 37
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR037375-1"
FT ACT_SITE 302
FT /evidence="ECO:0000256|PIRSR:PIRSR037375-1"
FT ACT_SITE 305
FT /evidence="ECO:0000256|PIRSR:PIRSR037375-1"
SQ SEQUENCE 634 AA; 65138 MW; 544D3A1387B99150 CRC64;
MKRFVLVVAL CAVSLFGALS PAGAAGRFNQ FVGLGDSTLD SGYFRYASSG NAAVNAQLLA
AIAGGAQGGF AGPGVMTSTM LAGRFGLGAQ PSSAGGGNYA NGSAYSALLS AAPGQPATPG
NLPGNVATTQ QIAGFLASVG GAVNPNALYV VNTGNNDLIF VQRQGADWIA ANPGFLGGLA
NQLAGSVAAL QAAGARTIIV PNSFYTATLT GLGGVLPAAN AADYARAFSY GQMKWSALSA
AGVRYIPADL HSLFRYVSVN PGLFGFTPSS VLASNAPSPV AALVTSWADI TPLQMQTFLF
IDGKHLTTAG QQIESDYEYS LLTAPVLMSL LAEGPVQGGL SRAATIQGQI DLSGRHRGEN
GVHVWATAGA GSLRMQTSSG FGEASGVPFA GSAGADYQTA FGLILGAAFT AGTQTQDFSQ
GAGRYDQNEQ AFSLYTAYQK GPVWGNAVAS YGLYQDKIRR EVALGLFTDH NSADTTGDSL
GLALRLGADL QWGALTTGPV AGLVLQRVTI QGFTESGTSG VTALSFGEQR RDSAVSQLGW
RVQADVGRFQ PFAEAKWHHE LADPKRKVKA SLTTAAAPSY SMDAAPVAVD WGALMLGANV
KINDRVMLRA SFSSMFGNPQ VNTCGGELGV NVSF
//