ID B6B000_9RHOB Unreviewed; 514 AA.
AC B6B000;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Probable lipid II flippase MurJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN Name=mviN {ECO:0000313|EMBL:EDZ42459.1};
GN Synonyms=murJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN ORFNames=RB2083_1974 {ECO:0000313|EMBL:EDZ42459.1};
OS Rhodobacteraceae bacterium HTCC2083.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=314270 {ECO:0000313|EMBL:EDZ42459.1, ECO:0000313|Proteomes:UP000005746};
RN [1] {ECO:0000313|Proteomes:UP000005746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2083 {ECO:0000313|Proteomes:UP000005746};
RX PubMed=21036993; DOI=10.1128/JB.01268-10;
RA Kang I., Vergin K.L., Oh H.M., Choi A., Giovannoni S.J., Cho J.C.;
RT "Genome sequence of strain HTCC2083, a novel member of the marine clade
RT Roseobacter.";
RL J. Bacteriol. 193:319-320(2011).
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 inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_02078}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_02078}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the MurJ/MviN family. {ECO:0000256|HAMAP-
CC Rule:MF_02078, ECO:0000256|PIRNR:PIRNR002869}.
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DR EMBL; DS995276; EDZ42459.1; -; Genomic_DNA.
DR AlphaFoldDB; B6B000; -.
DR STRING; 314270.RB2083_1974; -.
DR eggNOG; COG0728; Bacteria.
DR HOGENOM; CLU_006797_5_0_5; -.
DR OrthoDB; 9816572at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000005746; 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 inner membrane {ECO:0000256|HAMAP-Rule:MF_02078};
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}; Reference proteome {ECO:0000313|Proteomes:UP000005746};
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 92..114
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 134..153
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 165..183
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 189..208
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 229..250
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 270..291
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 312..335
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 347..365
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 385..404
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 410..427
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 448..471
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 477..504
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ SEQUENCE 514 AA; 55278 MW; F4FFC1A87F4C393A CRC64;
MSKNRMIVGV FTVGLWTLLS RVMGFVRDAL ILSYLGTGPA YQAFVVAFRL PNMFRRFFAE
GAFNLAFVPM FAKRLEADDQ PNAFANEAFS GLASVLIALT IIAQIFMPWL VYALASGFAG
TETFDLSVIF GRIAFPYILF ISLAALASGV LNAAGRFAAA AAAPVLLNVL LVSAILCAAY
AGFDVAFALI WMIPLAGFAQ LMLVWIAARR AGITLRLQRP RFTPDMKHLV KIAVPAAMAG
GVMQINLLVG QQVASYFDRA VGWLFAADRL YQLPLGVVGI AVGIVLLPDL SRRLQAGDEA
GAKDAFSRAT EISLALTIPA SVALMVIALP LVSVLFERGA LTSDDSAAIA VAVTIYGFGL
PAFVLQKTLQ PLFYAREDTK SPFRFALIAM AVNAVLAFGL TPYIGWLAPA IATTFAGWVM
VLCLALGTRP MGDVARFDAQ LKRRIWRICA ASAAMGTILW SASASMSTFL GMAGWRYLAL
AILIGIGMLS YFVIAHLTGA IRLSELKGAM RRRR
//
