ID   BTUC_ECOL6              Reviewed;         326 AA.
AC   Q8FH26;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Vitamin B12 import system permease protein BtuC;
GN   Name=btuC; OrderedLocusNames=c2107;
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: Part of the ABC transporter complex BtuCDF involved in
CC       vitamin B12 import. Involved in the translocation of the substrate
CC       across the membrane (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (BtuD),
CC       two transmembrane proteins (BtuC) and a solute-binding protein (BtuF).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. FecCD subfamily. {ECO:0000305}.
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DR   EMBL; AE014075; AAN80567.1; -; Genomic_DNA.
DR   RefSeq; WP_000956506.1; NC_004431.1.
DR   AlphaFoldDB; Q8FH26; -.
DR   SMR; Q8FH26; -.
DR   STRING; 199310.c2107; -.
DR   EnsemblBacteria; AAN80567; AAN80567; c2107.
DR   KEGG; ecc:c2107; -.
DR   eggNOG; COG4139; Bacteria.
DR   HOGENOM; CLU_013016_0_3_6; -.
DR   OMA; AMVYWSF; -.
DR   BioCyc; ECOL199310:C2107-MON; -.
DR   Proteomes; UP000001410; 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:0090482; F:vitamin transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015889; P:cobalamin transport; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.3470.10; -; 1.
DR   HAMAP; MF_01004; BtuC; 1.
DR   InterPro; IPR037294; ABC_BtuC-like.
DR   InterPro; IPR023691; ABC_transptr_BtuC.
DR   InterPro; IPR000522; ABC_transptr_permease_BtuC.
DR   PANTHER; PTHR30472; PTHR30472; 1.
DR   Pfam; PF01032; FecCD; 1.
DR   SUPFAM; SSF81345; SSF81345; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..326
FT                   /note="Vitamin B12 import system permease protein BtuC"
FT                   /id="PRO_0000059969"
FT   TOPO_DOM        1..10
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        11..35
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        36..56
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        57..81
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        82..92
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        93..107
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        108..113
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        114..138
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        139..141
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        142..166
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        167..190
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        191..206
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        207..228
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        229..249
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        250..257
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        258..267
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        268..274
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        275..296
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        297..304
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        305..324
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        325..326
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   326 AA;  34947 MW;  7E1387CE2DF43C5C CRC64;
     MLTLARQQQR QNIRWLLCLS VLMLLALLLS LCAGEQWILP GDWFSPRGEL FVWQIRLPRT
     LAVLLVGAAL AISGAVMQAL FENPLAEPGL LGVSNGAGVG LIAAVLLGQG QLPNWALGLC
     AIAGALIITL ILLRFARRHL STSRLLLAGV ALGIICSALM TWAIYFSTSV DLRQLMYWMM
     GGFGGVDWRQ SWLMVALIPV LLWICCQSRP MNMLALGEIS ARQLGLPLWF WRNVLVAATG
     WMVGVSVALA GAIGFIGLVI PHILRLCGLT DHRVLLPGCA LAGASALLLA DIVARLALAA
     AELPIGVVTA TLGAPVFIWL LLKAGR