TMPC_TREPA
ID TMPC_TREPA Reviewed; 353 AA.
AC P29724; O83339;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Membrane lipoprotein TmpC;
DE Short=Membrane protein C;
DE AltName: Full=35 kDa antigen;
DE AltName: Full=Lipoprotein TpN35;
DE AltName: Full=Purine nucleoside receptor A;
DE Short=PnrA;
DE Flags: Precursor;
GN Name=tmpC; OrderedLocusNames=TP_0319;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF CYS-21, DIACYLGLYCEROL AT
RP CYS-21, AND PALMITOYLATION AT CYS-21.
RC STRAIN=Nichols;
RX PubMed=1894360; DOI=10.1128/iai.59.10.3536-3546.1991;
RA Schouls L.M., van der Heide H.G.J., van Embden J.D.A.;
RT "Characterization of the 35-kilodalton Treponema pallidum subsp. pallidum
RT recombinant lipoprotein TmpC and antibody response to lipidated and
RT nonlipidated T. pallidum antigens.";
RL Infect. Immun. 59:3536-3546(1991).
RN [2]
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 36-353 IN COMPLEXES WITH
RP ADENOSINE; INOSINE AND GUANOSINE, PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP INDUCTION, AND SUBUNIT.
RX PubMed=16418175; DOI=10.1074/jbc.m511405200;
RA Deka R.K., Brautigam C.A., Yang X.F., Blevins J.S., Machius M.,
RA Tomchick D.R., Norgard M.V.;
RT "The PnrA (Tp0319; TmpC) lipoprotein represents a new family of bacterial
RT purine nucleoside receptor encoded within an ATP-binding cassette (ABC)-
RT like operon in Treponema pallidum.";
RL J. Biol. Chem. 281:8072-8081(2006).
CC -!- FUNCTION: Binds purine nucleosides and may play a role in purine
CC nucleoside uptake. May be part of an ABC-type nucleoside uptake system.
CC Has highest affinity for guanosine, followed by inosine and adenosine.
CC Has very low affinity for cytidine and does not bind thymidine.
CC {ECO:0000269|PubMed:16418175}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16418175}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- INDUCTION: Encoded in an operon with TP_0320, TP_0321, TP_0322 and
CC TP_0323 that may code for an ABC-type nucleoside uptake system, with
CC TP_0322 and/or TP_0323 encoding putative permeases, and TP_0319
CC encoding a ligand-binding protein. {ECO:0000269|PubMed:16418175}.
CC -!- SIMILARITY: Belongs to the BMP lipoprotein family. {ECO:0000305}.
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DR EMBL; X57836; CAA40968.1; -; Genomic_DNA.
DR EMBL; AE000520; AAC65302.1; -; Genomic_DNA.
DR PIR; H71340; H71340.
DR RefSeq; WP_010881767.1; NC_021490.2.
DR PDB; 2FQW; X-ray; 1.71 A; A=36-353.
DR PDB; 2FQX; X-ray; 1.70 A; A=36-353.
DR PDB; 2FQY; X-ray; 1.90 A; A=36-353.
DR PDBsum; 2FQW; -.
DR PDBsum; 2FQX; -.
DR PDBsum; 2FQY; -.
DR AlphaFoldDB; P29724; -.
DR SMR; P29724; -.
DR STRING; 243276.TPANIC_0319; -.
DR TCDB; 3.A.1.2.10; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; AAC65302; AAC65302; TP_0319.
DR KEGG; tpa:TP_0319; -.
DR eggNOG; COG1744; Bacteria.
DR HOGENOM; CLU_038813_0_0_12; -.
DR OMA; LASMMKR; -.
DR OrthoDB; 603910at2; -.
DR EvolutionaryTrace; P29724; -.
DR Proteomes; UP000000811; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR003760; PnrA-like.
DR Pfam; PF02608; Bmp; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Signal; Transport.
FT SIGNAL 1..20
FT CHAIN 21..353
FT /note="Membrane lipoprotein TmpC"
FT /id="PRO_0000018007"
FT BINDING 47..48
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /evidence="ECO:0000269|PubMed:16418175,
FT ECO:0007744|PDB:2FQY"
FT BINDING 47
FT /ligand="guanosine"
FT /ligand_id="ChEBI:CHEBI:16750"
FT /evidence="ECO:0000269|PubMed:16418175,
FT ECO:0007744|PDB:2FQX"
FT BINDING 47
FT /ligand="inosine"
FT /ligand_id="ChEBI:CHEBI:17596"
FT /evidence="ECO:0000269|PubMed:16418175,
FT ECO:0007744|PDB:2FQW"
FT BINDING 56
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /evidence="ECO:0000269|PubMed:16418175,
FT ECO:0007744|PDB:2FQY"
FT BINDING 57
FT /ligand="guanosine"
FT /ligand_id="ChEBI:CHEBI:16750"
FT /evidence="ECO:0000269|PubMed:16418175,
FT ECO:0007744|PDB:2FQX"
FT BINDING 57
FT /ligand="inosine"
FT /ligand_id="ChEBI:CHEBI:17596"
FT /evidence="ECO:0000269|PubMed:16418175,
FT ECO:0007744|PDB:2FQW"
FT BINDING 128
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /evidence="ECO:0000269|PubMed:16418175,
FT ECO:0007744|PDB:2FQY"
FT BINDING 128
FT /ligand="guanosine"
FT /ligand_id="ChEBI:CHEBI:16750"
FT /evidence="ECO:0000269|PubMed:16418175,
FT ECO:0007744|PDB:2FQX"
FT BINDING 128
FT /ligand="inosine"
FT /ligand_id="ChEBI:CHEBI:17596"
FT /evidence="ECO:0000269|PubMed:16418175,
FT ECO:0007744|PDB:2FQW"
FT BINDING 206
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /evidence="ECO:0000269|PubMed:16418175,
FT ECO:0007744|PDB:2FQY"
FT BINDING 206
FT /ligand="guanosine"
FT /ligand_id="ChEBI:CHEBI:16750"
FT /evidence="ECO:0000269|PubMed:16418175,
FT ECO:0007744|PDB:2FQX"
FT BINDING 232
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /evidence="ECO:0000269|PubMed:16418175,
FT ECO:0007744|PDB:2FQY"
FT BINDING 232
FT /ligand="guanosine"
FT /ligand_id="ChEBI:CHEBI:16750"
FT /evidence="ECO:0000269|PubMed:16418175,
FT ECO:0007744|PDB:2FQX"
FT BINDING 232
FT /ligand="inosine"
FT /ligand_id="ChEBI:CHEBI:17596"
FT /evidence="ECO:0000269|PubMed:16418175,
FT ECO:0007744|PDB:2FQW"
FT BINDING 258
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /evidence="ECO:0000269|PubMed:16418175,
FT ECO:0007744|PDB:2FQY"
FT BINDING 258
FT /ligand="guanosine"
FT /ligand_id="ChEBI:CHEBI:16750"
FT /evidence="ECO:0000269|PubMed:16418175,
FT ECO:0007744|PDB:2FQX"
FT BINDING 258
FT /ligand="inosine"
FT /ligand_id="ChEBI:CHEBI:17596"
FT /evidence="ECO:0000269|PubMed:16418175,
FT ECO:0007744|PDB:2FQW"
FT BINDING 280
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /evidence="ECO:0000269|PubMed:16418175,
FT ECO:0007744|PDB:2FQY"
FT BINDING 280
FT /ligand="guanosine"
FT /ligand_id="ChEBI:CHEBI:16750"
FT /evidence="ECO:0000269|PubMed:16418175,
FT ECO:0007744|PDB:2FQX"
FT BINDING 280
FT /ligand="inosine"
FT /ligand_id="ChEBI:CHEBI:17596"
FT /evidence="ECO:0000269|PubMed:16418175,
FT ECO:0007744|PDB:2FQW"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000269|PubMed:1894360"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305|PubMed:1894360"
FT MUTAGEN 21
FT /note="C->S: Loss of lipid incorporation and cleavage at
FT alternative processing site."
FT /evidence="ECO:0000269|PubMed:1894360"
FT CONFLICT 11
FT /note="G -> A (in Ref. 1; CAA40968)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="A -> R (in Ref. 1; CAA40968)"
FT /evidence="ECO:0000305"
FT STRAND 41..49
FT /evidence="ECO:0007829|PDB:2FQX"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2FQX"
FT HELIX 56..70
FT /evidence="ECO:0007829|PDB:2FQX"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:2FQX"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:2FQX"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:2FQX"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:2FQX"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:2FQX"
FT HELIX 109..118
FT /evidence="ECO:0007829|PDB:2FQX"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:2FQX"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:2FQX"
FT HELIX 144..161
FT /evidence="ECO:0007829|PDB:2FQX"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:2FQX"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:2FQX"
FT HELIX 179..192
FT /evidence="ECO:0007829|PDB:2FQX"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:2FQX"
FT HELIX 209..221
FT /evidence="ECO:0007829|PDB:2FQX"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:2FQX"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:2FQX"
FT HELIX 235..247
FT /evidence="ECO:0007829|PDB:2FQX"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:2FQX"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:2FQX"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:2FQX"
FT STRAND 272..280
FT /evidence="ECO:0007829|PDB:2FQX"
FT HELIX 282..294
FT /evidence="ECO:0007829|PDB:2FQX"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:2FQX"
FT TURN 308..311
FT /evidence="ECO:0007829|PDB:2FQX"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:2FQX"
FT HELIX 324..338
FT /evidence="ECO:0007829|PDB:2FQX"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:2FQX"
SQ SEQUENCE 353 AA; 37769 MW; CB373138C8C4337D CRC64;
MREKWVRAFA GVFCAMLLIG CSKSDRPQMG NAGGAEGGDF VVGMVTDSGD IDDKSFNQQV
WEGISRFAQE NNAKCKYVTA STDAEYVPSL SAFADENMGL VVACGSFLVE AVIETSARFP
KQKFLVIDAV VQDRDNVVSA VFGQNEGSFL VGVAAALKAK EAGKSAVGFI VGMELGMMPL
FEAGFEAGVK AVDPDIQVVV EVANTFSDPQ KGQALAAKLY DSGVNVIFQV AGGTGNGVIK
EARDRRLNGQ DVWVIGVDRD QYMDGVYDGS KSVVLTSMVK RADVAAERIS KMAYDGSFPG
GQSIMFGLED KAVGIPEENP NLSSAVMEKI RSFEEKIVSK EIVVPVRSAR MMN
