ID A0A148NBC3_9GAMM Unreviewed; 513 AA.
AC A0A148NBC3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=AXA67_04260 {ECO:0000313|EMBL:KXJ41806.1};
OS Methylothermaceae bacteria B42.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylothermaceae.
OX NCBI_TaxID=1798802 {ECO:0000313|EMBL:KXJ41806.1, ECO:0000313|Proteomes:UP000074680};
RN [1] {ECO:0000313|EMBL:KXJ41806.1, ECO:0000313|Proteomes:UP000074680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B42 {ECO:0000313|EMBL:KXJ41806.1};
RX PubMed=26779119; DOI=10.3389/fmicb.2015.01425;
RA Skennerton C.T., Ward L.M., Michel A., Metcalfe K., Valiente C., Mullin S.,
RA Chan K.Y., Gradinaru V., Orphan V.J.;
RT "Genomic Reconstruction of an Uncultured Hydrothermal Vent
RT Gammaproteobacterial Methanotroph (Family Methylothermaceae) Indicates
RT Multiple Adaptations to Oxygen Limitation.";
RL Front. Microbiol. 6:1425-1425(2015).
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}.
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:KXJ41806.1}.
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DR EMBL; LSNW01000006; KXJ41806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A148NBC3; -.
DR STRING; 1798802.AXA67_04260; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000074680; 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};
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 93..116
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 163..182
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 188..211
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 231..256
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 276..294
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 315..339
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 351..373
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 385..406
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 412..431
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 443..464
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 484..503
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ SEQUENCE 513 AA; 57141 MW; 05CF16E46E76675B CRC64;
MSRQLFKSTA VVGVWTLLSR ILGFIRDMVI ALLFGADSST DAFFVAFKIP NFMRRLFAEG
AFSQAFVPVM AEYKEKCGRE KLKEFLDRTA GSLALVLMLV TILGVIGAPW IIMMFAPGFV
WADGQYELAV NMLRITFPYL FFIASTALAG GILNTFNRFA VPAFTPVLLN LCLISAAFWL
APRLPEPIMG LAWGVFAAGA VQLLFQFPAL WRMKLLPRLR YGFHDPGVRK ILKLMLPALF
GVSITQINLL IDTLLASFLP HGSISWLYYS DRLVEFPLGV FGIALATVIL PNLSKDWAAG
RRASFSHAID WALRWVALIG LPAAVGLALL ARPILSALFQ YHAFTAHDVH MASMSLMAYS
MGLIGFIMVK ILVPGFTSRQ DTKTPVRFGV VAMIVNLILN LSLIWYLAHA GLALATSLAA
CVNGGLLLRR LRKEKVYQPS KGWWLFLLRI LLANAAMGAV LYYGTWHLEW ETWRLQQRML
QLGLWIGLGA LVYGGCLLVT GLRPRQLMMT RTR
//
