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Database: UniProt
Entry: MURJ_THEMA
LinkDB: MURJ_THEMA
Original site: MURJ_THEMA 
ID   MURJ_THEMA              Reviewed;         473 AA.
AC   Q9WXU1;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   RecName: Full=Probable lipid II flippase MurJ {ECO:0000255|HAMAP-Rule:MF_02078};
GN   Name=murJ {ECO:0000255|HAMAP-Rule:MF_02078}; Synonyms=mviN;
GN   OrderedLocusNames=TM_0086;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC   Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
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:0000255|HAMAP-Rule:MF_02078}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02078}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_02078}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_02078}.
CC   -!- SIMILARITY: Belongs to the MurJ/MviN family. {ECO:0000255|HAMAP-
CC       Rule:MF_02078}.
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DR   EMBL; AE000512; AAD35180.1; -; Genomic_DNA.
DR   PIR; H72419; H72419.
DR   RefSeq; NP_227902.1; NC_000853.1.
DR   RefSeq; WP_004082614.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q9WXU1; -.
DR   SMR; Q9WXU1; -.
DR   STRING; 243274.TM_0086; -.
DR   PaxDb; 243274-THEMA_04375; -.
DR   EnsemblBacteria; AAD35180; AAD35180; TM_0086.
DR   KEGG; tma:TM0086; -.
DR   eggNOG; COG0728; Bacteria.
DR   InParanoid; Q9WXU1; -.
DR   OrthoDB; 9804143at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015648; F:lipid-linked peptidoglycan transporter activity; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0034204; P:lipid translocation; IBA:GO_Central.
DR   GO; GO:0015836; P:lipid-linked peptidoglycan transport; IBA:GO_Central.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central.
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   PIRSF; PIRSF002869; MviN; 1.
DR   PRINTS; PR01806; VIRFACTRMVIN.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Membrane; Peptidoglycan synthesis;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..473
FT                   /note="Probable lipid II flippase MurJ"
FT                   /id="PRO_0000182016"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        253..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        300..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        327..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        360..380
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        382..402
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        414..434
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        439..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
SQ   SEQUENCE   473 AA;  51850 MW;  6D02DAD2D3FEBE5A CRC64;
     MSSIKKTLAF SLGTFFSRIT GLVRDIILAK TFGASSTLDA YYVSIVFPFF LRRTFAEGAM
     SSAFMAIYKK LKNKEEKAQF TSAVLTSLGL VTLLIVFLSE VFPYFMASIF ATGADEEVKS
     LAADLIRLTA PFITIVFVWA VFYSVHNASH RYFLPALTPM FSNVGVIVGC LFGDVRWAAA
     GFTIGGLAAL LVLLPFGKFR YRPTFKGLGE FYRLFFGTFM TMAVSQVTTL IDVNVASFLD
     PGSLSLIQLS SRLYQLPLGI FGVAVSTVAL STLSESEGDF HENLKDFISK SLFLTLPSSI
     GLMALSERII SLLFGYGAFT HEDVKKSAQI LFMYAIGLCF VSLFNLLSRA YHASKEVKTP
     FFATLLVSAV NISLDVILGF TMGASGIALA TSVSYIAGFV FLTLRMKPSF DKKIFKISLA
     SAVMGTVILL LRGSFKGNLG TIFLVLIGVF VYVLFSKLLK IEELEEILRR GSH
//
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