Y397_CLOPE
ID Y397_CLOPE Reviewed; 452 AA.
AC P50487; P94653;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Putative purine permease CPE0397;
GN Name=cpx; OrderedLocusNames=CPE0397;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 143-452.
RC STRAIN=ATCC 12917 / NCTC 8239 / Type A;
RX PubMed=8162194; DOI=10.1099/13500872-140-1-97;
RA Brynestad S., Iwanejko L.A., Stewart G.S., Granum P.E.;
RT "A complex array of Hpr consensus DNA recognition sequences proximal to the
RT enterotoxin gene in Clostridium perfringens type A.";
RL Microbiology 140:97-104(1994).
RN [3]
RP SEQUENCE REVISION.
RA Brynestad S.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC
CC 2.A.40) family. {ECO:0000305}.
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DR EMBL; BA000016; BAB80103.1; -; Genomic_DNA.
DR EMBL; X71844; CAA50688.1; -; Genomic_DNA.
DR RefSeq; WP_003473969.1; NC_003366.1.
DR AlphaFoldDB; P50487; -.
DR SMR; P50487; -.
DR STRING; 195102.gene:10489653; -.
DR TCDB; 2.A.40.2.1; the nucleobase/ascorbate transporter (nat) or nucleobase:cation symporter-2 (ncs2) family.
DR EnsemblBacteria; BAB80103; BAB80103; BAB80103.
DR KEGG; cpe:CPE0397; -.
DR HOGENOM; CLU_017959_8_2_9; -.
DR OMA; RKSAPFF; -.
DR Proteomes; UP000000818; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015205; F:nucleobase transmembrane transporter activity; IEA:UniProt.
DR InterPro; IPR006043; NCS2.
DR InterPro; IPR017588; UacT-like.
DR InterPro; IPR006042; Xan_ur_permease.
DR Pfam; PF00860; Xan_ur_permease; 1.
DR TIGRFAMs; TIGR00801; ncs2; 1.
DR TIGRFAMs; TIGR03173; pbuX; 1.
DR PROSITE; PS01116; XANTH_URACIL_PERMASE; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..452
FT /note="Putative purine permease CPE0397"
FT /id="PRO_0000165974"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 143..146
FT /note="VTGT -> ARVP (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="V -> I (in Ref. 2; CAA50688)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="P -> S (in Ref. 2; CAA50688)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="C -> M (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 269..278
FT /note="AIGETSNIDI -> SYWRDILLLIF (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="K -> T (in Ref. 2; CAA50688)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 452 AA; 46776 MW; 5CDAA29505357279 CRC64;
MEKQNLKNTE VNLIYGVDDD LDLPKKVLFG LQHIFAAFGG IIVVPLVIAT SLGFDSKVTT
ALISASILGS GLATIIQAKG VGKVGARVAC IMGTDFTFVS PAISVGSVLG LPGIIGATIL
GSLFEVILSF FIKPLMKFFP PLVTGTVVAL IGLTLLPVSI DWAAGGAGSA NYASLENLAV
AMFVLVITLL LNNYGKGMIS SASILIGIVV GYIVCIPLGL VDFTPVKEAS WLSFPKILEF
GVTFDAKAVM AFIPAYFVAT IGTVGCLKAI GETSNIDIGD KRVAAGVLSD GVGSALGGLV
GSCPNTSFSQ NIGIISLTKV ASRHVAVMAG ILLVILGFLP KVAAIITGIP NPVLGGVGIM
MFGTVAAAGI RTLSNIKLTE RNLLIIAISM GLGLGVTFRP DVIHNLPEAI RMIFSSGIST
GTIAALILNA VLKESPTSME FENMYDEEKK AS