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Database: UniProt
Entry: A0A1W9USV6_9CHLR
LinkDB: A0A1W9USV6_9CHLR
Original site: A0A1W9USV6_9CHLR 
ID   A0A1W9USV6_9CHLR        Unreviewed;       545 AA.
AC   A0A1W9USV6;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=B6I35_02050 {ECO:0000313|EMBL:OQY24285.1};
OS   Anaerolineaceae bacterium 4572_32.2.
OC   Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae.
OX   NCBI_TaxID=1971624 {ECO:0000313|EMBL:OQY24285.1, ECO:0000313|Proteomes:UP000192785};
RN   [1] {ECO:0000313|Proteomes:UP000192785}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Seitz K., Teske A., Baker B.;
RT   "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT   hydrothermal sediment communities.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:OQY24285.1}.
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DR   EMBL; NBLW01000015; OQY24285.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W9USV6; -.
DR   STRING; 1971624.B6I35_02050; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000192785; 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        106..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        147..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        183..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        208..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        291..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        333..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        377..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        403..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        428..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        463..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        500..521
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ   SEQUENCE   545 AA;  57286 MW;  AED46E74EDE3656A CRC64;
     MARSGRMSTR WRNGLEKTRE ISLRRDVEVA QAAGVVALGN VVSRVLGLVR EMVKSGLFGA
     GPHVDALNAA IRVPSVLYDL LVGGMVSSAL IPVLSDYVIP ERRAELWRLL SVLISIASLA
     LCALVLLGEL LAPQIVRLLV EGLSPSYQAL AADLLRLALP AVIFLSLSSV LSGGLYALKR
     FTFPAFTAAI FNAGVVVVAL ALGRRWGVRS MAAGLLVGSA LQVAFQLPGL RGARVRFTLD
     FRHPALRRIG SLYLPILIGL AVDTLAVLLS YNLASRIGEG SISWMEYAAT IIQFPLGLVV
     TAVSIAILPT LSQYAEAEET GPFQTILAQG LRLVLALIIP ATVGLYVLAN PVIALSFEHG
     DFTPADTVAT AAALRCALLG LLFAAIDQPL IFAFYARKDT LTPALVGVGT TFLYVAMALV
     PWRMGALTLP LLVLVNSLKL AAHALAMLAL TRRRLGGLGD HGLWPLVLKA ALASLAMAAL
     TGGVMRFLAA SAPPGLVGEL LVVGGAGGVG VVVYGLLALA LRIKEIHLLR AVVGDGLNRL
     TGAGR
//
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