ID A0A1G2PLE4_TERXR Unreviewed; 570 AA.
AC A0A1G2PLE4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=A2682_03860 {ECO:0000313|EMBL:OHA49140.1};
OS Terrybacteria sp. (strain RIFCSPHIGHO2_01_FULL_58_15).
OC Bacteria; Candidatus Terrybacteria.
OX NCBI_TaxID=1802363 {ECO:0000313|EMBL:OHA49140.1, ECO:0000313|Proteomes:UP000178690};
RN [1] {ECO:0000313|EMBL:OHA49140.1, ECO:0000313|Proteomes:UP000178690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIFCSPHIGHO2_01_FULL_58_15 {ECO:0000313|Proteomes:UP000178690};
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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 -!- 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}.
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:OHA49140.1}.
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DR EMBL; MHST01000013; OHA49140.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2PLE4; -.
DR STRING; 1802363.A2682_03860; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000178690; 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-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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 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 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}; Transport {ECO:0000256|HAMAP-Rule:MF_02078}.
FT TRANSMEM 53..78
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 99..122
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 142..161
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 168..189
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 195..216
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 279..300
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 321..345
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 357..379
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 391..413
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 478..501
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ SEQUENCE 570 AA; 60635 MW; 4E5A53AC66033A99 CRC64;
MIDRIVNLLN HESSSITLAA LLLAAASFAA DILGLLRDRI LATSFGAGEL LDIYYLGFRI
PDLLLNLFVL GAMSSALLPV FAERYARDRE DAWKLAQNLF TLVALLLTGL AVVLFFILPW
LMPLIAPGFA APALERAVVV TRILLLSPIL FGLSSLASAI LHYFQRFLLY SLAPILYNIG
IIAGALLFAP RFGEAGLALG VVLGAAMHFA IQVPGLRSAG FRFRFSLTPF HDAVREVGKL
ALPRTLNLVA NQLQLTVLTA IASAFAAGSI AVFNFATNLA FVPVGVIGIS FATAAFPALS
RAAAAGDRRR FGATLLRTIQ QVLFFALPAS ALFLVLRAHI VRVVLGAGAF TWEDTRLTAA
LLAASAVGVA AYSLLPLLVR AFFATKDTLT PFVIAVASAL LTIGLTLGLR WGLDASSDFR
GLLGGVFRVA DLPDIRILAL PIAMTVAVTF QVSVLLFKLR RDFSGEELRH LASGAFRLAI
SSVAAGGTAW GTLQVVAGGV AQETFVGILL QGFAAGIAGA AVFFFFAFTF AFPEAQRLMA
AMRRSLPPLS AVLPRSGSNT DEEGRRGMEQ
//
