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MURJ_HAEIN
ID   MURJ_HAEIN              Reviewed;         510 AA.
AC   P44958;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=HI_0964;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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; L42023; AAC22623.1; -; Genomic_DNA.
DR   PIR; I64162; I64162.
DR   RefSeq; NP_439125.1; NC_000907.1.
DR   AlphaFoldDB; P44958; -.
DR   SMR; P44958; -.
DR   STRING; 71421.HI_0964; -.
DR   EnsemblBacteria; AAC22623; AAC22623; HI_0964.
DR   KEGG; hin:HI_0964; -.
DR   PATRIC; fig|71421.8.peg.1006; -.
DR   eggNOG; COG0728; Bacteria.
DR   HOGENOM; CLU_006797_5_3_6; -.
DR   OMA; IFFVAFK; -.
DR   PhylomeDB; P44958; -.
DR   BioCyc; HINF71421:G1GJ1-1005-MON; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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   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..510
FT                   /note="Probable lipid II flippase MurJ"
FT                   /id="PRO_0000182008"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        154..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        266..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        315..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        357..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        396..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        443..463
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        481..501
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
SQ   SEQUENCE   510 AA;  56165 MW;  7E9FDD75F162ECC0 CRC64;
     MTLLSRVLGL VRDVVIAHLI GAGAAADVFL FANRIPNFLR RLFAEGAFSQ AFVPVLAEYQ
     QSGDMNKTRE FIGKVSGTLG GLVSIVTILA MVGSPHVAAL FGMGWFTDWM NDGPDAHKFE
     QASLLLKITF PYLWFVTFVA FSGAVLNTIG KFGVMSFSPV LLNIAMIATA LFLAPQMDNP
     DLALAIGIFL GGLLQFLFQI PFMKQAGLLV KPKWAWRDEG VTKIRKLMIP ALFGVSVSQI
     NLLLDTVIAS FLMTGSISWL YYSDRLLEFP LGLFGIAIST VILPTLARHH VNREGDSAKS
     AVDFRNTMDW GVRMIFLLGV PAAIGIAVLA QPMLLTLFMR GNFMLNDVYA ASYSLRAFNA
     GLLSFMLIKI LANGYYARQD TKTPVKIGII AMVSNMGFNL LAIPFSYVGL AIASAMSATL
     NAYLLYRGLA KADVYHFSRK SAVFFVKVLL AAIAMGAAVW YYVPEINQWA KMDFFMRVYW
     LVWLIVLAAI VYGATLILLG VRKHHLLTKN
 
 
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