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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//