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Database: UniProt
Entry: A0A1V4IY93_9CLOT
LinkDB: A0A1V4IY93_9CLOT
Original site: A0A1V4IY93_9CLOT 
ID   A0A1V4IY93_9CLOT        Unreviewed;       516 AA.
AC   A0A1V4IY93;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Lipid II flippase {ECO:0000256|PIRNR:PIRNR002869};
GN   Name=murJ {ECO:0000313|EMBL:OPJ65042.1};
GN   ORFNames=CLORY_00420 {ECO:0000313|EMBL:OPJ65042.1};
OS   Clostridium oryzae.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1450648 {ECO:0000313|EMBL:OPJ65042.1, ECO:0000313|Proteomes:UP000190080};
RN   [1] {ECO:0000313|EMBL:OPJ65042.1, ECO:0000313|Proteomes:UP000190080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28571 {ECO:0000313|EMBL:OPJ65042.1,
RC   ECO:0000313|Proteomes:UP000190080};
RA   Poehlein A., Daniel R.;
RT   "Genome sequence of Clostridium oryzae DSM 28571.";
RL   Submitted (MAR-2017) 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   -!- 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:OPJ65042.1}.
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DR   EMBL; MZGV01000001; OPJ65042.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4IY93; -.
DR   STRING; 1450648.CLORY_00420; -.
DR   Proteomes; UP000190080; 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:UP000190080};
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        12..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        49..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        83..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        130..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        181..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        218..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        260..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        303..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        349..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        375..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        401..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        434..457
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        469..489
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   516 AA;  56504 MW;  141527C74CF9B6F0 CRC64;
     MNKSRIARNS ILISIILILS KAAGFLRELV IAVIYGATRE SDIFKISTTI PTVIFSCIAS
     TIVTTFIPVF ATIKQDKKIA NEFFSNILNI VSIAAILLSV ISIIISPLLV TLFASGFTGK
     DFTVTVRLTR IALPSIIFLA IASLYTAYLQ SYEIFLQPSL TDMAASLVII LGILAFRNEG
     VTAAVISVLA GAMIQIVVQR PFIKNFKYKP IVNFKDKYIL QIITLGVPVF MSNIVGQFSV
     ILNRTMVSRL EAGSISVIDY AAKISTIINQ VFVVSVVTVL YPMLTEKFLK TDKTEFSNTV
     IKLIDMVFII SLPLISMLIV FGGPAVQILL MHGRFDSSAA AKTINCVKIL AVGTVGYGIL
     DTVSKVFFSA RKTKIPMYNS FITAVVNISL ILYLVPIFGV YGAALATAAT GIIMATVILL
     ELKYDMNFIR FSQCAFVFVK CALASVMIGV AANYVYFTVI KSLKYSENNY VIAFVILICV
     GLSAVIYIVT LRLMNVKEID IINDVLQKLG KIIACR
//
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