ID B1IJC3_CLOBK Unreviewed; 349 AA.
AC B1IJC3;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Putative membrane protein {ECO:0000313|EMBL:ACA43509.1};
GN OrderedLocusNames=CLD_3327 {ECO:0000313|EMBL:ACA43509.1};
OS Clostridium botulinum (strain Okra / Type B1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=498213 {ECO:0000313|EMBL:ACA43509.1, ECO:0000313|Proteomes:UP000008541};
RN [1] {ECO:0000313|EMBL:ACA43509.1, ECO:0000313|Proteomes:UP000008541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okra / Type B1 {ECO:0000313|Proteomes:UP000008541};
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP000939; ACA43509.1; -; Genomic_DNA.
DR RefSeq; WP_011948870.1; NC_010516.1.
DR AlphaFoldDB; B1IJC3; -.
DR GeneID; 5185496; -.
DR KEGG; cbb:CLD_3327; -.
DR HOGENOM; CLU_069616_0_0_9; -.
DR Proteomes; UP000008541; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR InterPro; IPR003352; PTS_EIIC.
DR PANTHER; PTHR40063; MEMBRANE PROTEIN-RELATED; 1.
DR PANTHER; PTHR40063:SF1; MEMBRANE PROTEIN-RELATED; 1.
DR Pfam; PF13303; PTS_EIIC_2; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 65..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 175..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..331
FT /note="Phosphotransferase system EIIC"
FT /evidence="ECO:0000259|Pfam:PF13303"
SQ SEQUENCE 349 AA; 35592 MW; CD5E26EC432BB5A8 CRC64;
MVIFKGTLLL LICLSAFSLF SLKAPKGMKA MGALADAAVA TFLVEAFQSY VGGDMLHIKL
LKDTGLAAGG MGGAAAATLV PLALGVSPVY AVLIGASCYG LGILPGFVAG YALSFIVPII
EKKVPKGLDL IVCVALVAPL ARLIGNGATP VVNSTLLNIG GIITVAANES PIIMGFILGG
VITVVATAPL SSMALTAMLG LKGLPMAIGA LSVMGSSFMN FVLFHRLKFG DRSTTISVAI
EPLTQADVIS ANPIPVYVTN FIGGGLAGII VTHFGLINNA TGTATPIAGL MVMYGFNDPK
TVTIAAIFCA LAGAFAGLLG SIVFKNYKIR TVAELRAASE EQEIEQATA
//
