ID J7QL95_METSZ Unreviewed; 509 AA.
AC J7QL95;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Probable lipid II flippase MurJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN Name=murJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN OrderedLocusNames=BN69_0377 {ECO:0000313|EMBL:CCJ05828.1};
OS Methylocystis sp. (strain SC2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylocystaceae; Methylocystis.
OX NCBI_TaxID=187303 {ECO:0000313|EMBL:CCJ05828.1, ECO:0000313|Proteomes:UP000005263};
RN [1] {ECO:0000313|EMBL:CCJ05828.1, ECO:0000313|Proteomes:UP000005263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:CCJ05828.1,
RC ECO:0000313|Proteomes:UP000005263};
RX PubMed=23045511; DOI=10.1128/JB.01446-12;
RA Dam B., Dam S., Kube M., Reinhardt R., Liesack W.;
RT "Complete Genome Sequence of Methylocystis sp. Strain SC2, an Aerobic
RT Methanotroph with High-Affinity Methane Oxidation Potential.";
RL J. Bacteriol. 194:6008-6009(2012).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE956757; CCJ05828.1; -; Genomic_DNA.
DR RefSeq; WP_014889862.1; NC_018485.1.
DR AlphaFoldDB; J7QL95; -.
DR STRING; 187303.BN69_0377; -.
DR KEGG; msc:BN69_0377; -.
DR PATRIC; fig|187303.17.peg.418; -.
DR eggNOG; COG0728; Bacteria.
DR HOGENOM; CLU_006797_5_0_5; -.
DR OMA; IFFVAFK; -.
DR OrthoDB; 9816572at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000005263; Chromosome.
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 49..69
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 81..102
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 122..144
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 156..179
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 185..204
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 225..248
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 268..285
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 306..324
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 344..366
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 378..397
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 403..424
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 436..457
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 469..499
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ SEQUENCE 509 AA; 53028 MW; A5B7C865DF150E0A CRC64;
MIRNLLSVGG FTLLSRVTGF LSLAMQSAIM GAGAVSDAFF IAQRLPNSFR AIFGEGAFSV
AFVPTYLMAI EKESDAAAEE FAGEVYTLLL ASQIILLAIV WALTPQFVSL IAPGLDDRPE
KFALAVNLTR ITFPYLLFIT LFVLHQGALN AHGRFALPAF AQNLMNLTVM AALAVAFLFP
NAGYAASWGV TVSGVLELGL LMWQARRIGV LQRLRRPHWS RVRDFFIRLG PAIIGSASPQ
IAVLADTILS SMLPDGGVSS ISYAERLYQL PVGVIGIAAG TVLLPEMSRR LAAGDEAGAL
HAQSRTMALT VAATAPFFIA FDTIPELIVA GLFQRGKFSA ADAYAAGDVL AAYGAGLMAL
VLIASARASF QARGDTRTPM LIALAALAAN VALKIVLFGP LGAVGLATAT SVGLWINLAA
LVGLALARDG MRFDAIFVKT LGATFVASAC LAAVAIFGRS SALALGAHFG ALANLVALTA
LAVVGALVYA GALLGALRAS GVTIASLRR
//