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MURJ_TREPA
ID   MURJ_TREPA              Reviewed;         526 AA.
AC   O83529;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 111.
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=TP_0516;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(1998).
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; AE000520; AAC65504.1; -; Genomic_DNA.
DR   PIR; C71315; C71315.
DR   RefSeq; WP_010881965.1; NC_021490.2.
DR   AlphaFoldDB; O83529; -.
DR   SMR; O83529; -.
DR   IntAct; O83529; 2.
DR   STRING; 243276.TPANIC_0516; -.
DR   EnsemblBacteria; AAC65504; AAC65504; TP_0516.
DR   GeneID; 57879039; -.
DR   KEGG; tpa:TP_0516; -.
DR   eggNOG; COG0728; Bacteria.
DR   HOGENOM; CLU_006797_5_0_12; -.
DR   OMA; IFFVAFK; -.
DR   OrthoDB; 749401at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000811; Chromosome.
DR   GO; GO:0005887; C:integral component of 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-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   Pfam; PF03023; MurJ; 1.
DR   PIRSF; PIRSF002869; MviN; 1.
DR   PRINTS; PR01806; VIRFACTRMVIN.
DR   TIGRFAMs; TIGR01695; murJ_mviN; 1.
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..526
FT                   /note="Probable lipid II flippase MurJ"
FT                   /id="PRO_0000182017"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        190..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        281..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        313..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        362..382
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        391..411
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        415..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        459..479
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        489..509
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
SQ   SEQUENCE   526 AA;  58052 MW;  A80B8434ECBC5D94 CRC64;
     MKSKSSLLKS GLLLSLLTLV SRVLGLAREV VKSTLMGTSA TADAFTVAFM IPNLFRRLFA
     ENAISVAFIP VFTQHYSMPS SAQVPCSSKT KEFLSAIFTL MSSVTASISL IGILGAPYIV
     RLFDTDQSLT VSLTRLMFPY LWMISLAAFF QGMLHSIKVF VPSGCTPIFF NVSVIFSMYF
     LNVSHMNVAI AAAIGVLIGG CAQALFQLIF VYMHGFRFTL QSPLKAMHDE GVRRIIALLL
     PTTVGIATYL LNDLVCTALA TSVEIGVAAS VQYSLRIQEL LLGIFIVSLS SVVLPDLSFH
     VMRKDWQSFE DLLITAIKIV MLITIPATFF VLFSSDRIIT LVYKNAIFNE LSVRMTATIF
     RWHSVGMLAI ALNRVLISAF YAQHNSFAPM IAGTISFVTN IILATLLFIP LGGKGIAFSL
     SAASMVQTVF LWMFLKRSWQ ITIPSLYKTS LYYGVKITLF SVIALVPTWA SSFFTAYFFP
     GSHKIISHGV PLCVEALIFS CTGCILLLLS RDEFAYKALR SIRFCR
 
 
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