ID A0A0U5IGV1_9GAMM Unreviewed; 1148 AA.
AC A0A0U5IGV1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=AMP-dependent synthetase and ligase {ECO:0000313|EMBL:CRI65277.1};
GN ORFNames=THIOKS12320015 {ECO:0000313|EMBL:CRI65277.1};
OS Thiocapsa sp. KS1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiocapsa.
OX NCBI_TaxID=610332 {ECO:0000313|EMBL:CRI65277.1, ECO:0000313|Proteomes:UP000198608};
RN [1] {ECO:0000313|Proteomes:UP000198608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KS1 {ECO:0000313|Proteomes:UP000198608};
RA Luecker S.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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; CVPF01000149; CRI65277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U5IGV1; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000198608; 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:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR CDD; cd06173; MFS_MefA_like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR43767; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR PANTHER; PTHR43767:SF1; NONRIBOSOMAL PEPTIDE SYNTHASE PES1 (EUROFUNG)-RELATED; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000313|EMBL:CRI65277.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 43..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 362..386
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 392..411
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 670..691
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 446..558
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 1148 AA; 124491 MW; 6D65F9D258E35004 CRC64;
MGQLFRITGF VAYIGMIFLN AFVDLGHKII IQNTLFKTYD GDAQILLTAI VNALILLPFV
LLFTPSGFLA DRFPKHLVMR ASAWVAVAVT LAIALFYYLA WFWAAFAMTF LLAVQSAFYS
PAKYGYIKEL VGKEALASAN GWVQATTTTA ILAGIFFFSV LFEGRLVGMS YTTPDEVMGM
MAPLGWVLVA GSLIEVVLAY RLPVRAPGTE MRFIWPDYAS GRYLRNNLHA AWDNQVIWLS
IVGLAIFWSI AQVILAAFPA FAKETLGETN TVVIQGVLAC SGIGIILGSV VAGRVSRNHI
ETGLIPVGAL GVSAALFVLP GLGSAWAHGL NFLLLGFLGG VFLVPLNALI QFNAGEQGLG
RVLAANNFIQ NIVMLSFLGL TVLAAYLKIG GLTVMLALAV VALCGAIYTL YQLPQSMVRF
LMARAMSTHY RLDVIGLKNM PAQGGVLMLG NHISWVDWAM VQMASPRPVR FVMERVIYER
WYLRWFLDFF GVVPISGGRS REAIETVSRL LDAGEVVCIF PEGTISKNGQ LSEFKRGFER
SARAATSGVI LPFYLRGLWG SRFSYAKEKL KASRREGRTR DVLVAFGRPL PREASAEQVK
QAVFELSVTS WQTHIATLPT LPAAWLAAAK QRLGEVAVID SAGTRLTNRR LIAAVLLFAR
RIKRLAPEPA VGILLPASSA AAIANLAALL VGKQVVNLNY TASSEALLAG MRNAGVRHVV
TSERFLDKLQ QRGIDLDAAF TEATLHPMEA LRAEIGKAEA LALLGIGILL PARLLLWLFG
RPGRPDDTAA ILFSSGSEGT PKGIELSHRN IMANVRQISD VLNTEPDDLI LANLPPFHAF
GLTVTTFLPL LEGIPMVCHP DPTDAVGTAK AIARYRATVL CSTSTFLRLF IRNQRVHPLM
LQSVRVVVAG AERLAPEVRD AFAIKFNKPI YEGYGATETT PVASVNVPDA METETWKIQA
GSRPGTVGLP LPGTSFRIVD PETLATLPPG EDGLILIGGV QVMKGYLNDP ERTADVVVEL
DGQRWYKTGD KGHLDPDGFL TIVDRYSRFA KLGGEMISLG AVEDQIRRIL GQPELELAAV
NLPDERKGER ILLLVAGEID ADGLRKQLLE AGMNPLSIPA EVLQVAAIPK LGSGKTDFGA
AKRLALAA
//
