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Database: UniProt
Entry: G2DG08_9GAMM
LinkDB: G2DG08_9GAMM
Original site: G2DG08_9GAMM 
ID   G2DG08_9GAMM            Unreviewed;       947 AA.
AC   G2DG08;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Peptide synthase {ECO:0000313|EMBL:EGV50437.1};
GN   ORFNames=Rifp1Sym_dc00020 {ECO:0000313|EMBL:EGV50437.1};
OS   endosymbiont of Riftia pachyptila (vent Ph05).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX   NCBI_TaxID=1048808 {ECO:0000313|EMBL:EGV50437.1, ECO:0000313|Proteomes:UP000004491};
RN   [1] {ECO:0000313|EMBL:EGV50437.1, ECO:0000313|Proteomes:UP000004491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D.,
RA   Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., Hecker M.,
RA   Sievert S.M., Schweder T.;
RT   "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and Tevnia
RT   jerichonana share an identical physiology as revealed by proteogenomic
RT   analyses.";
RL   ISME J. 0:0-0(2011).
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:EGV50437.1}.
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DR   EMBL; AFOC01000082; EGV50437.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2DG08; -.
DR   PATRIC; fig|1048808.3.peg.2582; -.
DR   Proteomes; UP000004491; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR   CDD; cd05931; FAAL; 1.
DR   CDD; cd07989; LPLAT_AGPAT-like; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR040097; FAAL/FAAC.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   PANTHER; PTHR22754:SF32; DISCO-INTERACTING PROTEIN 2; 1.
DR   PANTHER; PTHR22754; DISCO-INTERACTING PROTEIN 2 DIP2 -RELATED; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        715..735
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          19..96
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          96..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   947 AA;  104817 MW;  384C292057E17B5D CRC64;
     MAPSMEAPQQ LHSEKHAATP LLEIIATLAR ELHPLQTAWR PPTLDSHLER DLGFDSLGRL
     ELVARLERQF GVSLPEQSFA EAETPRDLLR AILSSPTTTS LEGTPPVIPE AGRSNEAPEQ
     AGSLTEMLDW HVAHHGERTH IRLYSDSDEG ERISYRQLHE GALKVAAALQ RHGLQPGEAV
     CLMLPTGSDY FYSFFGVLYA GGVPVPIYPP LRPSQLQDHL RRQISILSNA KATYLITIEA
     AKSLAKLLKA EVESLRELLT LDALHGNPQA LSPVILRSID TAFLQYTSGS TGTPKGVILT
     HANLLANIRA DGAAIEANAS DIFVSWLPLY HDMGLIGAWL GSLYFGAQLV IMSPLSFLAK
     PERWLWAIHR YGGTLSAAPN FAYQLCCSRI DDKALEGLDL SRWRVALNGA EAVSPETVQS
     FQARFSAYGF HAEALCPVYG LAESSVGLTF PPLHRKPLID RIRRLEFSRS GQAIAAEPDD
     PRALRFVACG HPLPHHEVRV VNAASHELPE RQQGAIQFRG PSACSGYFHN SQATRELFDG
     EWLRSGDLGY FADGDLFITG RSKDVIIRAG RNIYPEELEE AIGNLEGIRK GRVAIFSSQN
     QNQPGERLVI LAETREQDPA KREALSARID SIATYLTMIA PDEIILAAPG IILKTSSGKI
     RRGACRTLFE QGAIKAHPRP VWQQQLQLSL STLPNRIRRI VGSAKDWAYS LYTRGIFYIL
     AAFTYLSVML LPTTFRWPLM RAMARLLAKA SGTRLTLRGA EYLPTVTQPV ILVANHCSYL
     DGIALVALLP FSFRFVAKSE LRRNWIAHTF LKRINTLFVE RSDPRQAVTD SDTAQRSALQ
     GESQCYFPEG TFSRRPGLLP FHMGAFSTAA NAALPVQPIT IRGTRSILHA NDWFIHPSQI
     SLTLCEPVVP VPGIEDAWQQ AILLRDRART EILRHCGEPD LASEKRV
//
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