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Database: UniProt
Entry: A0A0G1FAZ7_9BACT
LinkDB: A0A0G1FAZ7_9BACT
Original site: A0A0G1FAZ7_9BACT 
ID   A0A0G1FAZ7_9BACT        Unreviewed;       564 AA.
AC   A0A0G1FAZ7;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   08-NOV-2023, entry version 24.
DE   RecName: Full=Lipid II flippase {ECO:0000256|PIRNR:PIRNR002869};
GN   ORFNames=UW02_C0009G0023 {ECO:0000313|EMBL:KKT19470.1};
OS   Candidatus Nomurabacteria bacterium GW2011_GWB1_43_7.
OC   Bacteria; Candidatus Nomurabacteria.
OX   NCBI_TaxID=1618747 {ECO:0000313|EMBL:KKT19470.1, ECO:0000313|Proteomes:UP000034751};
RN   [1] {ECO:0000313|EMBL:KKT19470.1, ECO:0000313|Proteomes:UP000034751}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- FUNCTION: Involved in peptidoglycan biosynthesis. Transports lipid-
CC       linked peptidoglycan precursors from the inner to the outer leaflet of
CC       the cytoplasmic membrane. {ECO:0000256|PIRNR:PIRNR002869}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the MurJ/MviN family.
CC       {ECO:0000256|PIRNR:PIRNR002869}.
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:KKT19470.1}.
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DR   EMBL; LCGS01000009; KKT19470.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1FAZ7; -.
DR   STRING; 1618747.UW02_C0009G0023; -.
DR   Proteomes; UP000034751; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0015648; F:lipid-linked peptidoglycan transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-UniRule.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-UniRule.
DR   CDD; cd13123; MATE_MurJ_like; 1.
DR   InterPro; IPR004268; MurJ.
DR   PANTHER; PTHR47019; LIPID II FLIPPASE MURJ; 1.
DR   PANTHER; PTHR47019:SF1; LIPID II FLIPPASE MURJ; 1.
DR   Pfam; PF03023; MurJ; 1.
DR   PIRSF; PIRSF002869; MviN; 1.
DR   PRINTS; PR01806; VIRFACTRMVIN.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|PIRNR:PIRNR002869};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|PIRNR:PIRNR002869};
KW   Cell wall biogenesis/degradation {ECO:0000256|PIRNR:PIRNR002869};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR002869};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984,
KW   ECO:0000256|PIRNR:PIRNR002869};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|PIRNR:PIRNR002869}.
FT   TRANSMEM        62..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        96..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        138..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        168..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        195..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        246..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        278..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        322..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        358..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        393..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        438..458
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        470..493
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        513..535
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   564 AA;  61972 MW;  A2B3A1B59F56B137 CRC64;
     MEKILRIFTK ESGSINQAAL LLGSFTLLSQ ILALFRDRAM AHFIGPSPSL DAYYAAFRVP
     DLIFISIASL ASITVIIPFI VAKMSGEQVT ESARKYLNDV FTVFFALMVS VALIAFIIMP
     NLVSFIAPGF TPLYQAKVIL LSRIMLFSPI LLGLSNLFGA VTQLFRKFFI YSLSPIFYNL
     GIIIGVLFLY PIFGIAGLAL GVVLGALLHF GVQALASHSS GFTPRFSFSI NFRDIRQVAI
     TSLPRTLGLA FNNIALIIII ALASFLKSGS ISVFNFSFNL QSVPLNIIGV SYAVAAFPAL
     AKSFGSGKTE EFKKHLKGAA RAIVFWSLPV IFLFIVLRAQ IVRVILGSGS FSWEDTRLVA
     ACLAIFSVSV LAQGMITLLS RSYYAAGNTR RPLIINFLCS LSIIILSYVF IYVFKNVTVF
     RYFMESLLKV EGIPGTEVLM LPLAYSAGTI LNFILHLIFI KKDFMSEELF ITKTFFQSLG
     ASFVLGLVSY LSLNALSPVF GTTTFLGTTF LGIFFQGLIS GVMGVLAATA VLYLLQNEEL
     RDLLKALRTK FWRAKVLAPS QEEL
//
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