ID   MDTP_ECOL6              Reviewed;         488 AA.
AC   Q8CVH8;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Multidrug resistance outer membrane protein MdtP;
DE   Flags: Precursor;
GN   Name=mdtP; OrderedLocusNames=c5085;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Could be involved in resistance to puromycin, acriflavine and
CC       tetraphenylarsonium chloride. {ECO:0000250}.
CC   -!- SUBUNIT: Could be part of a tripartite efflux system composed of MdtN,
CC       MdtO and MdtP. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC   -!- SIMILARITY: Belongs to the outer membrane factor (OMF) (TC 1.B.17)
CC       family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN83510.1; -; Genomic_DNA.
DR   RefSeq; WP_000610612.1; NC_004431.1.
DR   AlphaFoldDB; Q8CVH8; -.
DR   SMR; Q8CVH8; -.
DR   STRING; 199310.c5085; -.
DR   EnsemblBacteria; AAN83510; AAN83510; c5085.
DR   KEGG; ecc:c5085; -.
DR   eggNOG; COG1538; Bacteria.
DR   HOGENOM; CLU_012817_6_3_6; -.
DR   OMA; MSMNYAL; -.
DR   BioCyc; ECOL199310:C5085-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015562; F:efflux transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   InterPro; IPR003423; OMP_efflux.
DR   InterPro; IPR010131; RND_efflux_OM_lipoprot_NodT.
DR   Pfam; PF02321; OEP; 2.
DR   TIGRFAMs; TIGR01845; outer_NodT; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Cell outer membrane; Lipoprotein; Membrane;
KW   Palmitate; Signal; Transmembrane; Transmembrane beta strand.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           24..488
FT                   /note="Multidrug resistance outer membrane protein MdtP"
FT                   /id="PRO_0000031011"
FT   LIPID           24
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           24
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   488 AA;  53476 MW;  14BA246DC68C8E26 CRC64;
     MINRQLSRLL LCSILGSTTL ISGCALVRKD SAPHQQLKPE QIKLADDIHL ASSGWPQAQW
     WKQLNDPQLD SLIQRTLSGS HPLAEAKLRE EKAQSQADLL DAGSQLQVAA LGMLNRQRVS
     ANGFLSPYAM DAPALGMDGP YYTEATVGLF AGLDLDLWGV HRSAVAAAIG AHNAALAETA
     AVELSLTTGV AQLYYSMQAS YQMLDLLEQT RDVIDYAVKA HQSKVAHGLE AQVPFHGARA
     QILAVDKQIA AVKGQITETR ESLRALIGAG ASDMPEIKPV ALPRVQTGIP ATLSYELLAR
     RPDLQAMRWY VQASLDQVDS ARALFYPSFD IKAFFGLDSI HLDTLFKKTS RQFNFIPGLK
     LPLFDGGRLN ANLEGTRAAS NMMIERYNQS VLNAVRDVAV NGTRLQTLND EREMQAERVE
     ATRFTQRAAE AAYQRGLTSR LQATEARLPV LAEEMSLLML DSRRVIQSIQ LMKSLGGGYQ
     AAPIVEKK