ID E1IG40_9CHLR Unreviewed; 506 AA.
AC E1IG40;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=OSCT_2291 {ECO:0000313|EMBL:EFO79838.1};
OS Oscillochloris trichoides DG-6.
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Oscillochloridaceae; Oscillochloris.
OX NCBI_TaxID=765420 {ECO:0000313|EMBL:EFO79838.1, ECO:0000313|Proteomes:UP000054010};
RN [1] {ECO:0000313|EMBL:EFO79838.1, ECO:0000313|Proteomes:UP000054010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG-6 {ECO:0000313|EMBL:EFO79838.1,
RC ECO:0000313|Proteomes:UP000054010};
RX PubMed=21037015; DOI=10.1128/JB.00931-10;
RA Kuznetsov B.B., Ivanovsky R.N., Keppen O.I., Sukhacheva M.V.,
RA Bumazhkin B.K., Patutina E.O., Beletsky A.V., Mardanov A.V., Baslerov R.V.,
RA Panteleeva A.N., Kolganova T.V., Ravin N.V., Skryabin K.G.;
RT "Draft genome sequence of the anoxygenic filamentous phototrophic bacterium
RT Oscillochloris trichoides subsp. DG-6.";
RL J. Bacteriol. 193:321-322(2011).
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:EFO79838.1}.
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DR EMBL; ADVR01000099; EFO79838.1; -; Genomic_DNA.
DR AlphaFoldDB; E1IG40; -.
DR STRING; 765420.OSCT_2291; -.
DR eggNOG; COG0728; Bacteria.
DR HOGENOM; CLU_006797_5_2_0; -.
DR OrthoDB; 9804143at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000054010; 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; PTHR43486; LIPID II FLIPPASE MURJ-RELATED; 1.
DR PANTHER; PTHR43486:SF1; LIPID II FLIPPASE MURJ-RELATED; 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|HAMAP-Rule:MF_02078,
KW ECO:0000256|PIRNR:PIRNR002869};
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|HAMAP-Rule:MF_02078,
KW ECO:0000256|PIRNR:PIRNR002869};
KW Reference proteome {ECO:0000313|Proteomes:UP000054010};
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 81..107
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 127..149
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 182..204
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 224..243
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 263..281
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 342..366
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 378..396
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 402..424
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 444..471
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 477..499
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ SEQUENCE 506 AA; 52792 MW; 60DF310D56F78345 CRC64;
MRSIAIAALL IGIGNIASRA LGLIREPAIA YYFGRGAATD AFTLAWTVPN TIYDMLINGA
VSAALVPVFS EYAEGDRDEF WRVVSGVVTI ALAALSLLTA LVVWQAPAVV GLLVQSSQPE
LRAQTTSLVQ LLMPAVLLMG VSGLTTAILH AQQRFLLPAF VGATFNAGMI AGIMLLHQRY
GVNSLAGGAV IGAMGQAMIQ LPGLRGARLR PSFSLRHPAV RRILRLYAPV ALGIGFSIIG
TLIDRWLASG LPAAPTTMRY ATTLIQFPLG LVASAVALAV LPTLSRQSAS GDEAAFRSTL
AMGLKVVLLL ILPATAGLWA LAEPITALLF ERGAFGSSDS VATATALLYY LPGLPAAAID
QVLIFAFYSR KNTLTPNLIQ GAAIGFYLLV ALPLLAFSQL GFLALVLGNS AQWIGHALLA
AWLLQRIVPM GGQRLGEASL KGVLASLLMA LACAGVAALL HTQAALIQVL VAGGVGAGVY
LAASASLKIE ALGFFVAAVR ARLERR
//
