ID C6JM59_FUSVA Unreviewed; 1118 AA.
AC C6JM59;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Transporter, major facilitator family protein {ECO:0000313|EMBL:EES63822.1};
GN ORFNames=FVAG_02970 {ECO:0000313|EMBL:EES63822.1};
OS Fusobacterium varium ATCC 27725.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=469618 {ECO:0000313|EMBL:EES63822.1, ECO:0000313|Proteomes:UP000004505};
RN [1] {ECO:0000313|EMBL:EES63822.1, ECO:0000313|Proteomes:UP000004505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27725 {ECO:0000313|EMBL:EES63822.1,
RC ECO:0000313|Proteomes:UP000004505};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C.E.,
RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusobacterium varium ATCC 27725.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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:EES63822.1}.
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DR EMBL; ACIE02000034; EES63822.1; -; Genomic_DNA.
DR RefSeq; WP_005951651.1; NZ_GL988002.1.
DR AlphaFoldDB; C6JM59; -.
DR STRING; 469618.FVAG_02970; -.
DR GeneID; 77469106; -.
DR eggNOG; COG0204; Bacteria.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_008489_2_0_0; -.
DR Proteomes; UP000004505; 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: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; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR PANTHER; PTHR43201:SF5; MEDIUM-CHAIN ACYL-COA LIGASE ACSF2, MITOCHONDRIAL; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000004505};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 47..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 218..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 322..345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 357..380
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 386..412
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 674..695
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 446..556
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 1118 AA; 125290 MW; 3F2F63A655CFBCD5 CRC64;
MLLKNKRFCP LFITQFFGAF NDNMLKTAIM AFITYNLTLN RAHEGMLLNF ISILFILPFF
FLSATAGQLA DKYHRDKIAK ILKCIEFVLM LLTAVAVFFK FYSGLIIILF FMSVQSAFFG
PVKYSIIPQH LEECELIEGN AIIDGATYFS ILIGTILGAH ITSPNITVGI LVFCSLVGML
SSFKIPSAPA PRPDLSMSFN IFKTLRLTLK KISEIRSIYI TILGLSWFWA LGAVILTQLY
PMCSDLLGLS RNAVAVFMFI FSLGMAAGTF VCTKVMRGIV HPTFVPLSSI GIGIATFFLY
LFTKDYVTPD THIGTVVFFK SIPGIKISFI LFFLAFFGGM YIVPLNAFLQ NKAPKKYLAT
IIAGNNIMNA VGIVIFSALV LGLFKIGFII SDIFFLISII CLCVSLYILT IIPDALPRSM
AQSILSLIFK MEVTGLENYE KAGKRVLIIA NHTSLLDGLL VASFMPEKLI FAINTTISKK
WWIRIFKPVV KLYPIDPTNP LALKQLINEL KNNEKCIIFP EGRITVTGSL MKVYEGAGVV
ALKANANILP IRIDGAQYSK FSYLKTKLKT KFFPRIKITI LPPTKIKLSE DDKGSTKRGK
IGDQLYEIMT SMIFKSSPVR ENVFKSLLNA AKIHGKKHMI AEDIARQPMN YRNFILKSYV
IGEAIKRNFK EKNIGIVLPN SIINALVFFG LQSIGKIPAM INFTQGKSQI LSCIKTAEIS
TIITAKKMIE MLQLEELIKT LEENGVKIIY LEEFQSKINL ITKLSAFLNY LLKKVPQINY
NDPCTILFTS GSEGIPKAVL LSHENLQANR FQISSLFSFT SQDILFNALP MFHSFGLGIG
TILPLLSGIK VFFYPSPVHY KIVPELVYDS NSTILCGTDT FFNGYAKQAN PYDFYNIKYA
IVGAEKLKDS TYYQWLERFG VRVLEGYGVT EASPVISVNT PMHQKRGSVG RLLPDIEYKL
EAVPGIEKGG RLWIKGKNIM LGYLKDGKIT QPEGGWYDTG DIVDIDENKF ITILGRAKRF
AKIAGEMVSL TAVEEIINGY IKDFSNAVIS IPDEKKGEQL VLVTEKENVD TKDILNYFKE
KLYSELWVPK KIITVDKLPL LGTGKIDYIK VKEIVENQ
//
