ID A0A163ZNR6_9SYNE Unreviewed; 555 AA.
AC A0A163ZNR6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-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 ECO:0000313|EMBL:KZR86683.1};
GN ORFNames=MITS9508_02601 {ECO:0000313|EMBL:KZR86683.1};
OS Synechococcus sp. MIT S9508.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1801629 {ECO:0000313|EMBL:KZR86683.1, ECO:0000313|Proteomes:UP000076799};
RN [1] {ECO:0000313|EMBL:KZR86683.1, ECO:0000313|Proteomes:UP000076799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT S9508 {ECO:0000313|EMBL:KZR86683.1,
RC ECO:0000313|Proteomes:UP000076799};
RA Cubillos-Ruiz A., Berta-Thompson J.W., Becker J.W., Chisholm S.W.;
RT "Evolutionary Radiation of Lanthipeptides in Marine Picocyanobacteria.";
RL Submitted (FEB-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 -!- 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:KZR86683.1}.
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DR EMBL; LVHU01000015; KZR86683.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163ZNR6; -.
DR STRING; 1801629.MITS9508_02601; -.
DR PATRIC; fig|1801629.3.peg.2814; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000076799; 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; PTHR43486; LIPID II FLIPPASE MURJ-RELATED; 1.
DR PANTHER; PTHR43486:SF1; LIPID II FLIPPASE MURJ-RELATED; 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}; Cell shape {ECO:0000256|HAMAP-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|HAMAP-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 28..56
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 62..80
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 101..125
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 145..166
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 175..198
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 210..231
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 339..362
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 374..393
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 414..432
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 444..468
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 489..508
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 514..536
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ SEQUENCE 555 AA; 58514 MW; A1202BE5B2B1EAC6 CRC64;
MVPGDGPKIS FIDGMVQQAS MGRSLKRIAL VVTYGTLLSK AGGLIRQLVI AAAFGVGAAY
DAYNYAYILP GFLLILLGGI NGPFHSAMVS VLSRRPREEG AHILATLNTT VSALLLVVTA
VLVLAADPLI TLVGPGLPSD LHQIAVAQLQ VMAPMALLAG LIGLGFGSLN AADEFWIPAI
SPLMSSVALV LGVGLLWWQL GAEIALPVNA LWGGVVLGLS TLVGALLQWL LQLPALARQG
MARLRLSWDW SHPGVREVWR VMGPATLSSG MLQINVFTDM FFASGILGAA AGLSYSNLLV
QTPLGLISNA LLVPLLPTFS RLTAPEDRLP LIARIRQGLM LSTASMLPLG ALFLALSTPI
VALVYERGAF DQQAVQLVTG LLMTYGIGMP AYLGRDVLVR VFYALGDGTT PFRLSMAGIG
LNVLFDWALV GGPSPWGPQF PINLGAPGLV LATVLINLLT CLALLLALQK RLAGLPLREW
GLDALKLTLA AVAAGLAAWA LSLVVAWPEN FVGRLFQVGL SGALGLLLFV LCAQALSVPE
VSEISRGIAS RFRRR
//
