ID A0A0G0C920_9BACT Unreviewed; 557 AA.
AC A0A0G0C920;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 08-NOV-2023, entry version 27.
DE RecName: Full=Probable lipid II flippase MurJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN Name=murJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN ORFNames=UR38_C0003G0050 {ECO:0000313|EMBL:KKP47645.1};
OS Candidatus Woesebacteria bacterium GW2011_GWA2_33_28.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1618561 {ECO:0000313|EMBL:KKP47645.1, ECO:0000313|Proteomes:UP000033995};
RN [1] {ECO:0000313|EMBL:KKP47645.1, ECO:0000313|Proteomes:UP000033995}
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|HAMAP-Rule:MF_02078,
CC ECO:0000256|PIRNR:PIRNR002869}.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02078}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_02078};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_02078}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the MurJ/MviN family. {ECO:0000256|HAMAP-
CC Rule:MF_02078, 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:KKP47645.1}.
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; LBOZ01000003; KKP47645.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0C920; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000033995; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 HAMAP; MF_02078; MurJ_MviN; 1.
DR InterPro; IPR004268; MurJ.
DR NCBIfam; TIGR01695; murJ_mviN; 1.
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, ECO:0000256|HAMAP-
KW Rule:MF_02078};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_02078};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02078,
KW ECO:0000256|PIRNR:PIRNR002869};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02078};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW Rule:MF_02078};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_02078};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_02078};
KW Transport {ECO:0000256|HAMAP-Rule:MF_02078, ECO:0000256|PIRNR:PIRNR002869}.
FT TRANSMEM 16..37
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 57..81
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 93..117
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 137..160
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 167..188
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 194..216
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 319..337
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 357..376
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 388..409
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 415..436
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 448..470
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 501..523
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ SEQUENCE 557 AA; 61957 MW; 0A54590BE51651A7 CRC64;
MIFTKLKKII FAKQHTVLSA ATLIMVMIVV SRVLGLVRQR VLAHYFVPDD LSLFFAAFRL
PDTIFEVLVF GTFASAFIPV FSKSLKESKK NAWKLAGLIA NWGGLFFVAI TTIVIVFAHP
IYRVITPGFS NIDQETIVLM ARILFAAQGF FVISYVLTAV LESSKRFFVP ALAPLFYNLG
IILVTIFFSK ELGLLAPALG VVVGAGSHFL IQLPLARKLG FRFNRSLAIT SEVKKIAKLS
LPRIIEVSFL QIAKFVELTL ASLISIPAYT YFTFGNTIQL LPVGLFGTSI AKAALPTLAS
QADNLDAFKK TLFETLNQVV FLMAPMVAFL IVARVPVVRL IFGTDIFTWE STVETSLVVS
AFAIGIFSQA ANSILARSFY ALHDTKTPVI VSISTLFLNI LMDYLFVIVY KLPVWSLAFA
FSVAVLIQSG ILFGLIVKRI HNGIKRTLYI PVIKSLTGGI ISGGVMFFIL KFFDKSVWIK
KLSFISNLDL PFEKFVLDTR YTGNLLILTT IVGVIGVLVY IFILKLLKSK ELETFVNLFK
RMLTGQKFTT EFERSDL
//
