ID   A0A1G8ZHA0_9BACI        Unreviewed;       511 AA.
AC   A0A1G8ZHA0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Lipid II flippase {ECO:0000256|PIRNR:PIRNR002869};
GN   ORFNames=SAMN05216243_2012 {ECO:0000313|EMBL:SDK14408.1};
OS   Sediminibacillus albus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Sediminibacillus.
OX   NCBI_TaxID=407036 {ECO:0000313|EMBL:SDK14408.1, ECO:0000313|Proteomes:UP000198694};
RN   [1] {ECO:0000313|EMBL:SDK14408.1, ECO:0000313|Proteomes:UP000198694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.6502 {ECO:0000313|EMBL:SDK14408.1,
RC   ECO:0000313|Proteomes:UP000198694};
RA   de Groot N.N.;
RL   Submitted (OCT-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|PIRNR:PIRNR002869}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the MurJ/MviN family.
CC       {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; FNFL01000003; SDK14408.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8ZHA0; -.
DR   STRING; 407036.SAMN05216243_2012; -.
DR   Proteomes; UP000198694; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
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   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,
KW   ECO:0000256|PIRNR:PIRNR002869};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|PIRNR:PIRNR002869};
KW   Cell wall biogenesis/degradation {ECO:0000256|PIRNR:PIRNR002869};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR002869};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984,
KW   ECO:0000256|PIRNR:PIRNR002869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198694};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|PIRNR:PIRNR002869}.
FT   TRANSMEM        40..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        86..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        121..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        223..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        268..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        307..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        347..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        376..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        407..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        439..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        465..487
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   511 AA;  55571 MW;  28519668C6E627A6 CRC64;
     MLKSKLGMAS VLFLLTTLLL KISGLIRDMI IAFYFGDSYQ ADAFLAAFII PNMLFLFMTN
     GMKNALVPSY LEAASKGRAD SHLTQVLKGT AVVSAVLAAI GAGLSPYIIP LLYPGFSEQA
     QMIAVWVSVL LMSALVFVGI NAVLEAYLDA NNRFSIATVS QILVIAGMIL SAILFAEQIG
     PYALAAGYLI GAAVSLLFKL IFVVPKQTIN LREKINFKEV NAFYAIFIPV AVTVMVGQIN
     LAVDNIFAGQ FSEGTVTYIN YAKNLVHFPQ AIFGVTIATI VFPILAKAEA SDDRLLFKRT
     IAQGLTTMYL IVLPAVTGMM VLMPSIIGLL YERGAFTHQA TLATSQAAYY YFGSVLFFSL
     NTMINKGFYS LKKGKLIMGL GAASILFNVI FNYIFTRWLG YTGIPLASSV IGFLYIAIGF
     WIFLRLAGGL PLQMLGREFV KITIAALAML AGILPLISLL AEWPLAVSVI AIAGAGAIIY
     SVSAYLLRIE AMLFLWKNLR RKNNQKETTG R
//