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Database: UniProt
Entry: A0A1Y4GJ87_9BACT
LinkDB: A0A1Y4GJ87_9BACT
Original site: A0A1Y4GJ87_9BACT 
ID   A0A1Y4GJ87_9BACT        Unreviewed;       509 AA.
AC   A0A1Y4GJ87;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=B5F39_08880 {ECO:0000313|EMBL:OUO93100.1};
OS   Cloacibacillus sp. An23.
OC   Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC   Cloacibacillus.
OX   NCBI_TaxID=1965591 {ECO:0000313|EMBL:OUO93100.1, ECO:0000313|Proteomes:UP000196418};
RN   [1] {ECO:0000313|Proteomes:UP000196418}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An23 {ECO:0000313|Proteomes:UP000196418};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-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:OUO93100.1}.
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DR   EMBL; NFJQ01000008; OUO93100.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4GJ87; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000196418; 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}; Reference proteome {ECO:0000313|Proteomes:UP000196418};
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        85..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        129..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        180..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        221..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        269..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        307..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        339..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        376..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        401..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        442..460
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        472..493
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ   SEQUENCE   509 AA;  54866 MW;  2B7338E68DDADA8E CRC64;
     MVFHAMRMMA GTLVSRVLGL VREMLTAALF GATRQLDAFF VAYTLANLSR QLLAEGALSA
     SFVPVFSRTL AADGRDDARR LADEALTILI FGCSAVVAAG ILLSPFLVDI MAPGFAPEER
     AVAVTLTRMM FPFLMLVSVG ALAMGVLNSL GSFFVPAIAP ALSNLAYIIF LLATMRELSV
     WNLAFAVLTG GAFHMLLQVY WCSRLKFTLR PRRPDFADPQ LRGMMALFLP YAAGLSLNQL
     NPVISRMLGS FLDGGSISVL TYADRVLQLP LGLFVIAISQ AVLPVLSRQD PNDTASFCDF
     VRGAMRFNLF VVLPVAAGLC MVSHEVVHLL FFRGAFSEWA WHATGTALSL YALGLPGMAS
     STVIMRAIYA RRMPRAAVLV TGVTVAVNLA ASVVLMRFFA YAGLAAASAS AFTAASIFAA
     WKLSRNIGGR LRIFELSWLW RVLLPLAAMS AALAVFKKFM PYPDASALSA RLLWLFAATA
     GGGAVYAAGT LALRCPEWRW ICGAVKKRG
//
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