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Database: UniProt
Entry: A0A1G8YJC6_9ACTN
LinkDB: A0A1G8YJC6_9ACTN
Original site: A0A1G8YJC6_9ACTN 
ID   A0A1G8YJC6_9ACTN        Unreviewed;       535 AA.
AC   A0A1G8YJC6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
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=SAMN05421869_113293 {ECO:0000313|EMBL:SDK02898.1};
OS   Nonomuraea jiangxiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=633440 {ECO:0000313|EMBL:SDK02898.1, ECO:0000313|Proteomes:UP000199202};
RN   [1] {ECO:0000313|EMBL:SDK02898.1, ECO:0000313|Proteomes:UP000199202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.6533 {ECO:0000313|EMBL:SDK02898.1,
RC   ECO:0000313|Proteomes:UP000199202};
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|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}.
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DR   EMBL; FNDJ01000013; SDK02898.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8YJC6; -.
DR   STRING; 633440.SAMN05421869_113293; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000199202; 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}; Reference proteome {ECO:0000313|Proteomes:UP000199202};
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        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        87..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        130..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        164..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        195..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        241..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        280..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        323..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        362..384
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        396..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        424..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        466..487
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        493..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ   SEQUENCE   535 AA;  56404 MW;  0CCAF909002DF04C CRC64;
     MSRMLRASAI MAAGTMVSRV TGFVRTMVLA YAIGTAALGD SYNAAYAIPY SILDLLLLGV
     LSSVVVPMIV RAQHQDPDGG RAYEQRLLTI STVALVVVAA VAVLAAPLLI DLYTVWAPGS
     KRFEVGVTLA RFILPQLAFF GVGAVAGAIL NTRDRYGAPM WAPVLNNLVV ICVFLAYVVV
     GSGGGDIDKV TDGDLALLGL GTTAGIVAQA AVLIVALKRV GFSFVPRLDV WNARLGEMTK
     TGIWTIGYVV VTQLGFMLTV NLASSAGDVV PGHGISPYTL AFQLFQLPYG VIGVSVITAM
     LPRMSRAVAE ERFDDVRAEF GSSVRMICAL MVPVSLLLMV LGPAITVPIY GHGANSVADA
     VYIGNVLQVY GLALVPFSVF QLLLRVFYSF GDTRTPVFVG AGTTAVNAGL MVLFYSLLPA
     RYAVMGLALA YAIAYALGGV TAWWLASRRV QGLGGWTIGM ALTRMYLGAL PTAVLALAAV
     WVVTTAFDGL GFVNSLIVLG VGGGMGLLLY LAIAHRMRIP EVNSIVGMVA RRVGR
//
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