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Database: UniProt
Entry: A0A1T4PA26_9FIRM
LinkDB: A0A1T4PA26_9FIRM
Original site: A0A1T4PA26_9FIRM 
ID   A0A1T4PA26_9FIRM        Unreviewed;       507 AA.
AC   A0A1T4PA26;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-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=SAMN02745973_01982 {ECO:0000313|EMBL:SJZ88096.1};
OS   Garciella nitratireducens DSM 15102.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae; Garciella.
OX   NCBI_TaxID=1121911 {ECO:0000313|EMBL:SJZ88096.1, ECO:0000313|Proteomes:UP000196365};
RN   [1] {ECO:0000313|EMBL:SJZ88096.1, ECO:0000313|Proteomes:UP000196365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15102 {ECO:0000313|EMBL:SJZ88096.1,
RC   ECO:0000313|Proteomes:UP000196365};
RA   Peterson S.W.;
RL   Submitted (FEB-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}.
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DR   EMBL; FUWV01000015; SJZ88096.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4PA26; -.
DR   OrthoDB; 9804143at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000196365; 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:UP000196365};
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        38..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        83..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        122..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        153..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        178..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        265..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        303..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        344..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        374..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        399..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        433..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        466..486
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ   SEQUENCE   507 AA;  56201 MW;  62758132CC12D6B1 CRC64;
     MKKTAILLMI ITILSKILGF VREITLSYFY GASYISDAYL IALTIPGSIF AFISTGISTG
     YIPMYSNILK NKGIKEAEKF TNNIINLLFI VSTIIILIVV IFTQPIVKIF ASGFTGKTLD
     LAIRFTRVSI FSIYFIGLMY IFNSYLQLKN NFIAPAFNGF PFNMITIIII ALSAKINVAI
     LSVGSVLAYA FQFLYLLPFI RAKKYRYQLI FDIRDEHLKK LLFLALPVII GVSVNQINVI
     IDRTIASQIA IGGISALNYA QRLNGFIQGI FVVSIATVMY PAISKMAADH NIEGLKKSII
     DGIASISLMV IPATFGAMIF AQPIVKLLFG RGAFNKEALS MTSIALFFYS IGMIGFGFRE
     ILSRAFYSMQ DTKTPMMNAA LSMVLNIILN LILSKILGIG GLALSTSISA IFSTILLFIN
     LRKKVGPLGI KRFSITFIKI FISSLFMGII AKSSYNRLLM MLEDNLSILI SIGIGALVYA
     VIIYFMKIPE VDKMIQIIKG KFKKVKV
//
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