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Database: UniProt
Entry: A0A1M5CRP1_9FIRM
LinkDB: A0A1M5CRP1_9FIRM
Original site: A0A1M5CRP1_9FIRM 
ID   A0A1M5CRP1_9FIRM        Unreviewed;       529 AA.
AC   A0A1M5CRP1;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-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=SAMN02745218_02616 {ECO:0000313|EMBL:SHF57431.1};
OS   Desulfofundulus australicus DSM 11792.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulfofundulus.
OX   NCBI_TaxID=1121425 {ECO:0000313|EMBL:SHF57431.1, ECO:0000313|Proteomes:UP000184196};
RN   [1] {ECO:0000313|EMBL:SHF57431.1, ECO:0000313|Proteomes:UP000184196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11792 {ECO:0000313|EMBL:SHF57431.1,
RC   ECO:0000313|Proteomes:UP000184196};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; FQUW01000040; SHF57431.1; -; Genomic_DNA.
DR   RefSeq; WP_073167022.1; NZ_FQUW01000040.1.
DR   AlphaFoldDB; A0A1M5CRP1; -.
DR   OrthoDB; 9804143at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000184196; 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        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        86..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        128..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        161..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        227..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        267..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        308..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        346..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        380..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        406..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        439..469
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        475..497
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ   SEQUENCE   529 AA;  55020 MW;  BC518CAB04CA55A7 CRC64;
     MSRSNTIARA TAVIAVFTLL SKVLGFMREM ALACVFGASA ATDAYLVAYT VPNVIFAVLG
     GALTVTAVPL FASYASAGKR GEAWRLFAVF STLLSAILLA VVLAGMPLAR QIVWLVAPGL
     PEGTARLAAS LLAVMLPGVL FLSLANLFYG LLNASNIFGP PALGSVVTNI FIVASILAGL
     RFGITAVAAG TTLGYLAALV LQLPYLRRAG FIFRPSLEFR HPGLKRAFGL MFPVMVGTGI
     GQIYLIIDRV LASGLPEGSI SALNYASKLI LLPQGVLVMA LSTAIFPALS HKAASGDQAG
     FSHTLLRAVK TVLLVALPAG VGLAVLREPV VRLLFMRGAF DEDDLAMTVF ALLCFSLGLA
     GQCLGPVLTR GFYALQDTAT PVKVGVATVT LNLALSLVLV RPLAHGGLAL ANSLAATFNV
     AVLFYLLARR VPGLDVRGLL AFAAGAALAS FLAGGAAALA DGFLAGVLAG GTAALALRLA
     ADALAGVLVF AGACQVLKLD EYLYLKDLLR RAFQRGMSFI RARPLYRSR
//
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