ID A0A0G1ALB1_9BACT Unreviewed; 553 AA.
AC A0A0G1ALB1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 08-NOV-2023, entry version 25.
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=UU87_C0004G0047 {ECO:0000313|EMBL:KKS26063.1};
OS Parcubacteria group bacterium GW2011_GWA2_42_11.
OC Bacteria.
OX NCBI_TaxID=1618819 {ECO:0000313|EMBL:KKS26063.1, ECO:0000313|Proteomes:UP000033821};
RN [1] {ECO:0000313|EMBL:KKS26063.1, ECO:0000313|Proteomes:UP000033821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(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 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:KKS26063.1}.
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DR EMBL; LCCH01000004; KKS26063.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1ALB1; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000033821; 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 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 63..85
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 105..129
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 149..168
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 175..196
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 202..230
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 251..280
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 286..308
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 329..352
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 364..386
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 398..420
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 426..444
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 464..486
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 498..523
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ SEQUENCE 553 AA; 60841 MW; EC1E4945996C7A0F CRC64;
MNIFKSNFLN GQSRTITSAA IILAITSLAS RFLGLLRDRL LAGQFGAGDT LDVYYAAFRI
PDLVFNLLVF GALVAGFIPT FLSYWRADAG DNQKVSAEGW RFVNVILNLF FIVLLVIGGL
FFIFTPYLMK LITPGFNPEK LALTVQLTRM MFLSPLLLGL SSVFGGVLES LKRFLIFSLT
PIVYNFGIIF GVLFLVPRFG IYGLAGGVIL GAFFHLVIQI PAVWSLGWRY KFILDFKDKG
MRRVLGLMGP RVLTLAVGQL NFIAITIIAS ALAAGSLAIF NLSFNIWSFP LGIIAASLAI
AAFPTLTANA QMKNWSAFVG NFSTTFRQIF FLIIPSSALF IILRAQIVRV ALGSGKFNWE
NTILTAQSLM FLTFGLFAEA LIMLLVRGFF AVEDTKTPFW LGLVSSIFRI GCAWVFSLVW
GVAGLALGYS FGAIIYFLLL WVCLRRKIAR LSGSAQRHLN EKEIIISGLK IVAASLLAGA
AAWGMLRLID NFVDMQTLLG VFAQGFIAGL AGLAVYFLAG LLFRSQEMGT FWKAIKNRLP
FKAVAPDKEL IEP
//
