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MTRC_NEIGO
ID   MTRC_NEIGO              Reviewed;         412 AA.
AC   P43505;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Membrane fusion protein MtrC;
DE   Flags: Precursor;
GN   Name=mtrC;
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FA19;
RX   PubMed=8196548; DOI=10.1111/j.1365-2958.1994.tb00354.x;
RA   Pan W., Spratt B.G.;
RT   "Regulation of the permeability of the gonococcal cell envelope by the mtr
RT   system.";
RL   Mol. Microbiol. 11:769-775(1994).
CC   -!- FUNCTION: Cell membrane lipoprotein, involved in cell membrane
CC       permeability to hydrophobic compounds such as antibiotics, dyes and
CC       detergents.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC   -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC       family. {ECO:0000305}.
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DR   EMBL; U14993; AAA80193.1; -; Genomic_DNA.
DR   RefSeq; WP_003693766.1; NZ_UGRK01000002.1.
DR   AlphaFoldDB; P43505; -.
DR   SMR; P43505; -.
DR   TCDB; 2.A.6.2.5; the resistance-nodulation-cell division (rnd) superfamily.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   InterPro; IPR043602; CusB_dom_1.
DR   InterPro; IPR032317; HlyD_D23.
DR   InterPro; IPR006143; RND_pump_MFP.
DR   Pfam; PF00529; CusB_dom_1; 1.
DR   Pfam; PF16576; HlyD_D23; 1.
DR   TIGRFAMs; TIGR01730; RND_mfp; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Lipoprotein; Membrane; Palmitate;
KW   Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           25..412
FT                   /note="Membrane fusion protein MtrC"
FT                   /id="PRO_0000018713"
FT   REGION          377..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           25
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           25
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   412 AA;  42774 MW;  97F9AFBCFAE321BA CRC64;
     MAFYASKAMR AAALAAAVAL ALSSCGKGGD AAQGGQPAGR EAPAPVVGVV TVHPQTVALT
     VELPGRLESL RTADVRAQVG GIIQKRLFQE GSYVRAGQPL YQIDSSTYEA GLESARAQLA
     TAQATLAKAD ADLARYKPLV SADAISKQEY DAAVTAKRSA EASVKAAQAA IKSAGINLNR
     SRITAPISGF IGQSKVSEGT LLNAGDTTVL ATIRQTNPMY VNVTQSASEV MKLRRQIAEG
     KLLAADGAIA VGIKFDDGTV YPEKGRLLFA DPTVDESTGQ ITLRAAVSND QNILMPGLYV
     RVLMDQVAAD NAFIVPQQAV TRGAKDTVMI VNAQGGMEPR EVTVAQQQGT NWIVTSGLKD
     GDKVVVEGIS IAGMTGAKKV TPKEWAPSEN QAAAPQAGVQ TASEAKPASE AK
 
 
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