BTUC_ECOLI
ID BTUC_ECOLI Reviewed; 326 AA.
AC P06609; P77197;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Vitamin B12 import system permease protein BtuC;
GN Name=btuC; OrderedLocusNames=b1711, JW1701;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3528129; DOI=10.1128/jb.167.3.928-934.1986;
RA Friedrich M.J., Deveaux L.C., Kadner R.J.;
RT "Nucleotide sequence of the btuCED genes involved in vitamin B12 transport
RT in Escherichia coli and homology with components of periplasmic-binding-
RT protein-dependent transport systems.";
RL J. Bacteriol. 167:928-934(1986).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=2671656; DOI=10.1007/bf02464897;
RA Rioux C.R., Kadner R.J.;
RT "Vitamin B12 transport in Escherichia coli K12 does not require the btuE
RT gene of the btuCED operon.";
RL Mol. Gen. Genet. 217:301-308(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP CHARACTERIZATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11790740; DOI=10.1128/jb.184.3.706-717.2002;
RA Cadieux N., Bradbeer C., Reeger-Schneider E., Koester W., Mohanty A.K.,
RA Wiener M.C., Kadner R.J.;
RT "Identification of the periplasmic cobalamin-binding protein BtuF of
RT Escherichia coli.";
RL J. Bacteriol. 184:706-717(2002).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH BTUD.
RX PubMed=12004122; DOI=10.1126/science.1071142;
RA Locher K.P., Lee A.T., Rees D.C.;
RT "The E. coli BtuCD structure: a framework for ABC transporter architecture
RT and mechanism.";
RL Science 296:1091-1098(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.
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:0000269|PubMed:12004122}.
CC -!- INTERACTION:
CC P06609; P06609: btuC; NbExp=2; IntAct=EBI-1033427, EBI-1033427;
CC P06609; P06611: btuD; NbExp=13; IntAct=EBI-1033427, EBI-1033420;
CC P06609; P37028: btuF; NbExp=10; IntAct=EBI-1033427, EBI-1118724;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. FecCD subfamily. {ECO:0000305}.
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DR EMBL; M14031; AAA23526.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74781.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15479.1; -; Genomic_DNA.
DR PIR; G64929; QRECBC.
DR RefSeq; NP_416226.1; NC_000913.3.
DR RefSeq; WP_000956528.1; NZ_SSZK01000001.1.
DR PDB; 1L7V; X-ray; 3.20 A; A/B=1-326.
DR PDB; 2QI9; X-ray; 2.60 A; A/B=1-326.
DR PDB; 4DBL; X-ray; 3.49 A; A/B/F/G=1-326.
DR PDB; 4FI3; X-ray; 3.47 A; A/B=1-326.
DR PDB; 4R9U; X-ray; 2.78 A; A/B=1-326.
DR PDBsum; 1L7V; -.
DR PDBsum; 2QI9; -.
DR PDBsum; 4DBL; -.
DR PDBsum; 4FI3; -.
DR PDBsum; 4R9U; -.
DR AlphaFoldDB; P06609; -.
DR SMR; P06609; -.
DR BioGRID; 4263152; 131.
DR ComplexPortal; CPX-2105; Cobalamin ABC transporter complex.
DR ComplexPortal; CPX-2106; BtuCD complex.
DR DIP; DIP-9233N; -.
DR IntAct; P06609; 2.
DR MINT; P06609; -.
DR STRING; 511145.b1711; -.
DR TCDB; 3.A.1.13.1; the atp-binding cassette (abc) superfamily.
DR PaxDb; P06609; -.
DR PRIDE; P06609; -.
DR EnsemblBacteria; AAC74781; AAC74781; b1711.
DR EnsemblBacteria; BAA15479; BAA15479; BAA15479.
DR GeneID; 945877; -.
DR KEGG; ecj:JW1701; -.
DR KEGG; eco:b1711; -.
DR PATRIC; fig|1411691.4.peg.546; -.
DR EchoBASE; EB0125; -.
DR eggNOG; COG4139; Bacteria.
DR HOGENOM; CLU_013016_0_3_6; -.
DR InParanoid; P06609; -.
DR OMA; AMVYWSF; -.
DR PhylomeDB; P06609; -.
DR BioCyc; EcoCyc:BTUC-MON; -.
DR BioCyc; MetaCyc:BTUC-MON; -.
DR BRENDA; 7.6.2.8; 2026.
DR EvolutionaryTrace; P06609; -.
DR PRO; PR:P06609; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IDA:EcoCyc.
DR GO; GO:1990191; C:cobalamin transport complex; IPI:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IMP:EcoliWiki.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015889; P:cobalamin transport; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..326
FT /note="Vitamin B12 import system permease protein BtuC"
FT /id="PRO_0000059968"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT TRANSMEM 11..35
FT /note="Helical; Name=1"
FT TOPO_DOM 36..56
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT TRANSMEM 57..81
FT /note="Helical; Name=2"
FT TOPO_DOM 82..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT TRANSMEM 93..107
FT /note="Helical; Name=3"
FT TOPO_DOM 108..113
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT TRANSMEM 114..138
FT /note="Helical; Name=4"
FT TOPO_DOM 139..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT TRANSMEM 142..166
FT /note="Helical; Name=5"
FT TOPO_DOM 167..190
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT TRANSMEM 191..206
FT /note="Helical; Name=6"
FT TOPO_DOM 207..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT TRANSMEM 229..249
FT /note="Helical; Name=7"
FT TOPO_DOM 250..257
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT TRANSMEM 258..267
FT /note="Helical; Name=8"
FT TOPO_DOM 268..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT TRANSMEM 275..296
FT /note="Helical; Name=9"
FT TOPO_DOM 297..304
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT TRANSMEM 305..324
FT /note="Helical; Name=10"
FT TOPO_DOM 325..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT CONFLICT 111..112
FT /note="QL -> LT (in Ref. 1; AAA23526)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="A -> R (in Ref. 1; AAA23526)"
FT /evidence="ECO:0000305"
FT HELIX 3..31
FT /evidence="ECO:0007829|PDB:2QI9"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:4R9U"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:2QI9"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:4R9U"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:2QI9"
FT HELIX 56..80
FT /evidence="ECO:0007829|PDB:2QI9"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:2QI9"
FT HELIX 93..108
FT /evidence="ECO:0007829|PDB:2QI9"
FT HELIX 114..136
FT /evidence="ECO:0007829|PDB:2QI9"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:4R9U"
FT HELIX 142..165
FT /evidence="ECO:0007829|PDB:2QI9"
FT HELIX 171..179
FT /evidence="ECO:0007829|PDB:2QI9"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:2QI9"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:2QI9"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:2QI9"
FT HELIX 198..204
FT /evidence="ECO:0007829|PDB:2QI9"
FT HELIX 208..215
FT /evidence="ECO:0007829|PDB:2QI9"
FT HELIX 218..223
FT /evidence="ECO:0007829|PDB:2QI9"
FT HELIX 228..250
FT /evidence="ECO:0007829|PDB:2QI9"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:1L7V"
FT HELIX 259..265
FT /evidence="ECO:0007829|PDB:2QI9"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:2QI9"
FT HELIX 272..295
FT /evidence="ECO:0007829|PDB:2QI9"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:2QI9"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:4R9U"
FT HELIX 305..321
FT /evidence="ECO:0007829|PDB:2QI9"
SQ SEQUENCE 326 AA; 34949 MW; C65882B1C47BFE69 CRC64;
MLTLARQQQR QNIRWLLCLS VLMLLALLLS LCAGEQWISP GDWFTPRGEL FVWQIRLPRT
LAVLLVGAAL AISGAVMQAL FENPLAEPGL LGVSNGAGVG LIAAVLLGQG QLPNWALGLC
AIAGALIITL ILLRFARRHL STSRLLLAGV ALGIICSALM TWAIYFSTSV DLRQLMYWMM
GGFGGVDWRQ SWLMLALIPV LLWICCQSRP MNMLALGEIS ARQLGLPLWF WRNVLVAATG
WMVGVSVALA GAIGFIGLVI PHILRLCGLT DHRVLLPGCA LAGASALLLA DIVARLALAA
AELPIGVVTA TLGAPVFIWL LLKAGR
