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
//