BTUB_ECOLI
ID BTUB_ECOLI Reviewed; 614 AA.
AC P06129; Q2M8R1;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Vitamin B12 transporter BtuB {ECO:0000255|HAMAP-Rule:MF_01531};
DE AltName: Full=Cobalamin receptor {ECO:0000255|HAMAP-Rule:MF_01531};
DE AltName: Full=Outer membrane cobalamin translocator {ECO:0000255|HAMAP-Rule:MF_01531};
DE Flags: Precursor;
GN Name=btuB; Synonyms=bfe, cer, dcrC; OrderedLocusNames=b3966, JW3938;
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=3882670; DOI=10.1128/jb.161.3.904-908.1985;
RA Heller K., Kadner R.J.;
RT "Nucleotide sequence of the gene for the vitamin B12 receptor protein in
RT the outer membrane of Escherichia coli.";
RL J. Bacteriol. 161:904-908(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
RX PubMed=1999392; DOI=10.1128/jb.173.5.1757-1764.1991;
RA Gustafsson C., Lindstroem P.H.R., Hagervall T.G., Esberg K.B., Bjoerk G.R.;
RT "The trmA promoter has regulatory features and sequence elements in common
RT with the rRNA P1 promoter family of Escherichia coli.";
RL J. Bacteriol. 173:1757-1764(1991).
RN [6]
RP PROTEIN SEQUENCE OF 21-32.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 456-614.
RC STRAIN=B;
RX PubMed=8093236; DOI=10.1128/jb.175.1.111-116.1993;
RA Dougherty T.J., Thanassi J.A., Pucci M.J.;
RT "The Escherichia coli mutant requiring D-glutamic acid is the result of
RT mutations in two distinct genetic loci.";
RL J. Bacteriol. 175:111-116(1993).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=2982793; DOI=10.1128/jb.161.3.896-903.1985;
RA Heller K., Mann B.J., Kadner R.J.;
RT "Cloning and expression of the gene for the vitamin B12 receptor protein in
RT the outer membrane of Escherichia coli.";
RL J. Bacteriol. 161:896-903(1985).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF THE TONB BOX.
RX PubMed=2687240; DOI=10.1128/jb.171.12.6526-6533.1989;
RA Gudmundsdottir A., Bell P.E., Lundrigan M.D., Bradbeer C., Kadner R.J.;
RT "Point mutations in a conserved region (TonB box) of Escherichia coli outer
RT membrane protein BtuB affect vitamin B12 transport.";
RL J. Bacteriol. 171:6526-6533(1989).
RN [10]
RP INDUCTION, AND REGULATION OF EXPRESSION.
RC STRAIN=K12;
RX PubMed=9852020; DOI=10.1128/jb.180.24.6719-6728.1998;
RA Nou X., Kadner R.J.;
RT "Coupled changes in translation and transcription during cobalamin-
RT dependent regulation of btuB expression in Escherichia coli.";
RL J. Bacteriol. 180:6719-6728(1998).
RN [11]
RP FUNCTION, AND INTERACTION WITH TONB.
RC STRAIN=K12;
RX PubMed=10485884; DOI=10.1073/pnas.96.19.10673;
RA Cadieux N., Kadner R.J.;
RT "Site-directed disulfide bonding reveals an interaction site between
RT energy-coupling protein TonB and BtuB, the outer membrane cobalamin
RT transporter.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:10673-10678(1999).
RN [12]
RP MUTAGENESIS OF LEU-28 AND VAL-30.
RC STRAIN=K12;
RX PubMed=11705387; DOI=10.1021/bi015602p;
RA Coggshall K.A., Cadieux N., Piedmont C., Kadner R.J., Cafiso D.S.;
RT "Transport-defective mutations alter the conformation of the energy-
RT coupling motif of an outer membrane transporter.";
RL Biochemistry 40:13964-13971(2001).
RN [13]
RP CALCIUM-BINDING SITES AND SUBSTRATE-BINDING SITES, AND ACTIVITY REGULATION.
RX PubMed=14499604; DOI=10.1016/j.jmb.2003.07.005;
RA Chimento D.P., Kadner R.J., Wiener M.C.;
RT "The Escherichia coli outer membrane cobalamin transporter BtuB: structural
RT analysis of calcium and substrate binding, and identification of
RT orthologous transporters by sequence/structure conservation.";
RL J. Mol. Biol. 332:999-1014(2003).
RN [14]
RP CRYSTALLIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=12595710; DOI=10.1107/s0907444903000052;
RA Chimento D.P., Mohanty A.K., Kadner R.J., Wiener M.C.;
RT "Crystallization and initial X-ray diffraction of BtuB, the integral
RT membrane cobalamin transporter of Escherichia coli.";
RL Acta Crystallogr. D 59:509-511(2003).
RN [15] {ECO:0007744|PDB:1NQE, ECO:0007744|PDB:1NQF, ECO:0007744|PDB:1NQG, ECO:0007744|PDB:1NQH}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 21-614 OF NATIVE PROTEIN AND
RP COMPLEX WITH CALCIUM AND CYANOCOBALAMIN, SUBCELLULAR LOCATION, AND
RP TOPOLOGY.
RX PubMed=12652322; DOI=10.1038/nsb914;
RA Chimento D.P., Mohanty A.K., Kadner R.J., Wiener M.C.;
RT "Substrate-induced transmembrane signaling in the cobalamin transporter
RT BtuB.";
RL Nat. Struct. Biol. 10:394-401(2003).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 21-614 IN COMPLEX WITH COLICIN E3
RP RECEPTOR BINDING DOMAIN.
RX PubMed=14528295; DOI=10.1038/nsb997;
RA Kurisu G., Zakharov S.D., Zhalnina M.V., Bano S., Eroukova V.Y.,
RA Rokitskaya T.I., Antonenko Y.N., Wiener M.C., Cramer W.A.;
RT "The structure of BtuB with bound colicin E3 R-domain implies a
RT translocon.";
RL Nat. Struct. Biol. 10:948-954(2003).
CC -!- FUNCTION: Involved in the active translocation of vitamin B12
CC (cyanocobalamin) across the outer membrane to the periplasmic space. It
CC derives its energy for transport by interacting with the trans-
CC periplasmic membrane protein TonB. Is also a receptor for
CC bacteriophages BF23 and C1, and for A and E colicins.
CC {ECO:0000269|PubMed:10485884, ECO:0000269|PubMed:2687240,
CC ECO:0000269|PubMed:2982793}.
CC -!- ACTIVITY REGULATION: Calcium increases vitamin B12 binding affinity by
CC a factor of 50-100. {ECO:0000269|PubMed:14499604}.
CC -!- SUBUNIT: Interacts with TonB. {ECO:0000269|PubMed:10485884,
CC ECO:0000269|PubMed:14528295}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:12595710,
CC ECO:0000269|PubMed:12652322, ECO:0000269|PubMed:2687240,
CC ECO:0000269|PubMed:2982793}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12595710, ECO:0000269|PubMed:12652322,
CC ECO:0000269|PubMed:2687240, ECO:0000269|PubMed:2982793}.
CC -!- INDUCTION: Constitutively expressed. Primary control of btuB expression
CC by cobalamin occurs at the level of translation initiation.
CC {ECO:0000269|PubMed:9852020}.
CC -!- SIMILARITY: Belongs to the TonB-dependent receptor family. BtuB (TC
CC 1.B.14.3.1) subfamily. {ECO:0000255|HAMAP-Rule:MF_01531, ECO:0000305}.
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DR EMBL; M10112; AAA23524.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43072.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76948.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77345.1; -; Genomic_DNA.
DR EMBL; M57568; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L14556; AAA23676.1; -; Genomic_DNA.
DR PIR; A65204; QRECBT.
DR RefSeq; NP_418401.1; NC_000913.3.
DR RefSeq; WP_000591359.1; NZ_SSZK01000065.1.
DR PDB; 1NQE; X-ray; 2.00 A; A=21-614.
DR PDB; 1NQF; X-ray; 2.70 A; A=21-614.
DR PDB; 1NQG; X-ray; 3.31 A; A=21-614.
DR PDB; 1NQH; X-ray; 3.10 A; A=21-614.
DR PDB; 1UJW; X-ray; 2.75 A; A=21-614.
DR PDB; 2GSK; X-ray; 2.10 A; A=25-614.
DR PDB; 2GUF; X-ray; 1.95 A; A=21-614.
DR PDB; 2YSU; X-ray; 3.50 A; A=21-614.
DR PDB; 3M8B; X-ray; 2.44 A; A=21-614.
DR PDB; 3M8D; X-ray; 2.44 A; A=21-614.
DR PDB; 3RGM; X-ray; 2.60 A; A=21-614.
DR PDB; 3RGN; X-ray; 2.30 A; A=21-614.
DR PDB; 7NSU; EM; 4.70 A; F=21-614.
DR PDBsum; 1NQE; -.
DR PDBsum; 1NQF; -.
DR PDBsum; 1NQG; -.
DR PDBsum; 1NQH; -.
DR PDBsum; 1UJW; -.
DR PDBsum; 2GSK; -.
DR PDBsum; 2GUF; -.
DR PDBsum; 2YSU; -.
DR PDBsum; 3M8B; -.
DR PDBsum; 3M8D; -.
DR PDBsum; 3RGM; -.
DR PDBsum; 3RGN; -.
DR PDBsum; 7NSU; -.
DR AlphaFoldDB; P06129; -.
DR PCDDB; P06129; -.
DR SMR; P06129; -.
DR BioGRID; 4259524; 247.
DR ComplexPortal; CPX-1083; Cobalamin outer membrane transporter complex.
DR DIP; DIP-9232N; -.
DR IntAct; P06129; 1.
DR STRING; 511145.b3966; -.
DR DrugBank; DB04233; (Hydroxyethyloxy)Tri(Ethyloxy)Octane.
DR DrugBank; DB04039; 3-Oxo-Pentadecanoic Acid.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR TCDB; 1.B.14.3.1; the outer membrane receptor (omr) family.
DR jPOST; P06129; -.
DR PaxDb; P06129; -.
DR PRIDE; P06129; -.
DR EnsemblBacteria; AAC76948; AAC76948; b3966.
DR EnsemblBacteria; BAE77345; BAE77345; BAE77345.
DR GeneID; 948468; -.
DR KEGG; ecj:JW3938; -.
DR KEGG; eco:b3966; -.
DR PATRIC; fig|1411691.4.peg.2738; -.
DR EchoBASE; EB0124; -.
DR eggNOG; COG4206; Bacteria.
DR HOGENOM; CLU_008287_18_5_6; -.
DR InParanoid; P06129; -.
DR OMA; SYELQWR; -.
DR PhylomeDB; P06129; -.
DR BioCyc; EcoCyc:EG10126-MON; -.
DR BioCyc; MetaCyc:EG10126-MON; -.
DR EvolutionaryTrace; P06129; -.
DR PRO; PR:P06129; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0045203; C:integral component of cell outer membrane; IDA:EcoCyc.
DR GO; GO:0016021; C:integral component of membrane; IDA:CAFA.
DR GO; GO:0031230; C:intrinsic component of cell outer membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:1902495; C:transmembrane transporter complex; IC:ComplexPortal.
DR GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IDA:EcoCyc.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0015889; P:cobalamin transport; IDA:EcoCyc.
DR GO; GO:0034220; P:ion transmembrane transport; IDA:CAFA.
DR Gene3D; 2.170.130.10; -; 1.
DR Gene3D; 2.40.170.20; -; 1.
DR HAMAP; MF_01531; BtuB; 1.
DR InterPro; IPR010101; B12_transptr_BtuB.
DR InterPro; IPR039426; BtuB-like.
DR InterPro; IPR012910; Plug_dom.
DR InterPro; IPR037066; Plug_dom_sf.
DR InterPro; IPR000531; TonB-dep_rcpt_b-brl.
DR InterPro; IPR010916; TonB_box_CS.
DR InterPro; IPR036942; TonB_rcpt_b-brl_sf.
DR InterPro; IPR010917; TonB_rcpt_CS.
DR PANTHER; PTHR30069; PTHR30069; 1.
DR Pfam; PF07715; Plug; 1.
DR Pfam; PF00593; TonB_dep_Rec; 1.
DR TIGRFAMs; TIGR01779; TonB-B12; 1.
DR PROSITE; PS00430; TONB_DEPENDENT_REC_1; 1.
DR PROSITE; PS01156; TONB_DEPENDENT_REC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell outer membrane; Direct protein sequencing;
KW Ion transport; Membrane; Metal-binding; Porin; Receptor;
KW Reference proteome; Signal; TonB box; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 21..614
FT /note="Vitamin B12 transporter BtuB"
FT /id="PRO_0000003479"
FT TOPO_DOM 21..157
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:12652322"
FT TRANSMEM 158..165
FT /note="Beta stranded"
FT TOPO_DOM 166..168
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:12652322"
FT TRANSMEM 169..178
FT /note="Beta stranded"
FT TOPO_DOM 179..183
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:12652322"
FT TRANSMEM 184..195
FT /note="Beta stranded"
FT TOPO_DOM 196..216
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:12652322"
FT TRANSMEM 217..227
FT /note="Beta stranded"
FT TOPO_DOM 228..231
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:12652322"
FT TRANSMEM 232..248
FT /note="Beta stranded"
FT TOPO_DOM 249..262
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:12652322"
FT TRANSMEM 263..277
FT /note="Beta stranded"
FT TOPO_DOM 278
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:12652322"
FT TRANSMEM 279..296
FT /note="Beta stranded"
FT TOPO_DOM 297..308
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:12652322"
FT TRANSMEM 309..325
FT /note="Beta stranded"
FT TOPO_DOM 326..327
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:12652322"
FT TRANSMEM 328..337
FT /note="Beta stranded"
FT TOPO_DOM 338..352
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:12652322"
FT TRANSMEM 353..369
FT /note="Beta stranded"
FT TOPO_DOM 370
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:12652322"
FT TRANSMEM 371..381
FT /note="Beta stranded"
FT TOPO_DOM 382..384
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:12652322"
FT TRANSMEM 385..400
FT /note="Beta stranded"
FT TOPO_DOM 401..402
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:12652322"
FT TRANSMEM 403..417
FT /note="Beta stranded"
FT TOPO_DOM 418..433
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:12652322"
FT TRANSMEM 434..443
FT /note="Beta stranded"
FT TOPO_DOM 444..448
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:12652322"
FT TRANSMEM 449..458
FT /note="Beta stranded"
FT TOPO_DOM 459..472
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:12652322"
FT TRANSMEM 473..490
FT /note="Beta stranded"
FT TOPO_DOM 491..493
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:12652322"
FT TRANSMEM 494..509
FT /note="Beta stranded"
FT TOPO_DOM 510..516
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:12652322"
FT TRANSMEM 517..529
FT /note="Beta stranded"
FT TOPO_DOM 530..534
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:12652322"
FT TRANSMEM 535..550
FT /note="Beta stranded"
FT TOPO_DOM 551..557
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:12652322"
FT TRANSMEM 558..572
FT /note="Beta stranded"
FT TOPO_DOM 573..584
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:12652322"
FT TRANSMEM 585..596
FT /note="Beta stranded"
FT TOPO_DOM 597..601
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:12652322"
FT TRANSMEM 602..614
FT /note="Beta stranded"
FT MOTIF 26..33
FT /note="TonB box"
FT MOTIF 597..614
FT /note="TonB C-terminal box"
FT BINDING 83
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000269|PubMed:12652322,
FT ECO:0007744|PDB:1NQH"
FT BINDING 85
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000269|PubMed:12652322,
FT ECO:0007744|PDB:1NQH"
FT BINDING 92
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000269|PubMed:12652322,
FT ECO:0007744|PDB:1NQH"
FT BINDING 110..111
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000269|PubMed:12652322,
FT ECO:0007744|PDB:1NQH"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12652322"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12652322"
FT BINDING 213
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12652322"
FT BINDING 213
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12652322"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12652322"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12652322"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12652322"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12652322"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12652322"
FT BINDING 251
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000269|PubMed:12652322,
FT ECO:0007744|PDB:1NQH"
FT BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12652322"
FT BINDING 309
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000269|PubMed:12652322,
FT ECO:0007744|PDB:1NQH"
FT BINDING 517
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000269|PubMed:12652322,
FT ECO:0007744|PDB:1NQH"
FT BINDING 551
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000269|PubMed:12652322,
FT ECO:0007744|PDB:1NQH"
FT MUTAGEN 28
FT /note="L->P: Inactivates uptake."
FT /evidence="ECO:0000269|PubMed:11705387"
FT MUTAGEN 30
FT /note="V->G,P: Inactivates uptake."
FT /evidence="ECO:0000269|PubMed:11705387"
FT CONFLICT 162
FT /note="A -> G (in Ref. 1; AAA23524)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="A -> R (in Ref. 1; AAA23524)"
FT /evidence="ECO:0000305"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:2GUF"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:2GUF"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:2GUF"
FT HELIX 51..57
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:2GUF"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:2GUF"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:2GUF"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:1NQE"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:3RGN"
FT HELIX 112..118
FT /evidence="ECO:0007829|PDB:2GUF"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:2GUF"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 157..165
FT /evidence="ECO:0007829|PDB:2GUF"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 169..181
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 184..195
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:2GSK"
FT STRAND 217..248
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:1NQH"
FT STRAND 262..277
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 279..297
FT /evidence="ECO:0007829|PDB:2GUF"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:2GSK"
FT STRAND 309..325
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 327..343
FT /evidence="ECO:0007829|PDB:2GUF"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:1NQE"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 352..368
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 371..382
FT /evidence="ECO:0007829|PDB:2GUF"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 386..400
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 403..414
FT /evidence="ECO:0007829|PDB:2GUF"
FT HELIX 418..422
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 423..426
FT /evidence="ECO:0007829|PDB:1NQF"
FT STRAND 433..446
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 449..467
FT /evidence="ECO:0007829|PDB:2GUF"
FT TURN 468..471
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 472..492
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 495..508
FT /evidence="ECO:0007829|PDB:2GUF"
FT TURN 509..511
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 520..531
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 534..543
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 546..550
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 552..555
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 557..561
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 564..587
FT /evidence="ECO:0007829|PDB:2GUF"
FT STRAND 605..613
FT /evidence="ECO:0007829|PDB:2GUF"
SQ SEQUENCE 614 AA; 68407 MW; AB43CC46A991FF95 CRC64;
MIKKASLLTA CSVTAFSAWA QDTSPDTLVV TANRFEQPRS TVLAPTTVVT RQDIDRWQST
SVNDVLRRLP GVDITQNGGS GQLSSIFIRG TNASHVLVLI DGVRLNLAGV SGSADLSQFP
IALVQRVEYI RGPRSAVYGS DAIGGVVNII TTRDEPGTEI SAGWGSNSYQ NYDVSTQQQL
GDKTRVTLLG DYAHTHGYDV VAYGNTGTQA QTDNDGFLSK TLYGALEHNF TDAWSGFVRG
YGYDNRTNYD AYYSPGSPLL DTRKLYSQSW DAGLRYNGEL IKSQLITSYS HSKDYNYDPH
YGRYDSSATL DEMKQYTVQW ANNVIVGHGS IGAGVDWQKQ TTTPGTGYVE DGYDQRNTGI
YLTGLQQVGD FTFEGAARSD DNSQFGRHGT WQTSAGWEFI EGYRFIASYG TSYKAPNLGQ
LYGFYGNPNL DPEKSKQWEG AFEGLTAGVN WRISGYRNDV SDLIDYDDHT LKYYNEGKAR
IKGVEATANF DTGPLTHTVS YDYVDARNAI TDTPLLRRAK QQVKYQLDWQ LYDFDWGITY
QYLGTRYDKD YSSYPYQTVK MGGVSLWDLA VAYPVTSHLT VRGKIANLFD KDYETVYGYQ
TAGREYTLSG SYTF
