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Accession Number: | P06129 |
Protein Name: | BtuB aka BFE aka CER aka DCRC aka B3966 |
Length: | 614 |
Molecular Weight: | 68407.00 |
Species: | Escherichia coli [83333] |
Location1 / Topology2 / Orientation3: | Cell outer membrane1 / Multi-pass membrane protein2 |
Substrate | cyanocob(III)alamin |
Cross database links:
DIP: | DIP-9232N |
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RefSeq: | AP_003844.1 NP_418401.1 |
Entrez Gene ID: | 948468 |
Pfam: | PF07715 PF00593 |
BioCyc: | EcoCyc:EG10126-MONOMER ECOL168927:B3966-MONOMER |
KEGG: | ecj:JW3938 eco:b3966 |
Gene Ontology
GO:0009279
C:cell outer membrane
GO:0005886
C:plasma membrane
GO:0046930
C:pore complex
GO:0015235
F:cobalamin transporter activity
GO:0046872
F:metal ion binding
GO:0005515
F:protein binding
GO:0004872
F:receptor activity
GO:0015889
P:cobalamin transport
GO:0009597
P:detection of virus
GO:0046718
P:entry of virus into host cell
GO:0006811
P:ion transport
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References (15)[1] “Nucleotide sequence of the gene for the vitamin B12 receptor protein in the outer membrane of Escherichia coli.” Heller K.et.al. 3882670 [2] “Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes.” Blattner F.R.et.al. 8265357 [3] “The complete genome sequence of Escherichia coli K-12.” Blattner F.R.et.al. 9278503 [4] “Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.” Hayashi K.et.al. 16738553 [5] “The trmA promoter has regulatory features and sequence elements in common with the rRNA P1 promoter family of Escherichia coli.” Gustafsson C.et.al. 1999392 [6] “Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.” Link A.J.et.al. 9298646 [7] “The Escherichia coli mutant requiring D-glutamic acid is the result of mutations in two distinct genetic loci.” Dougherty T.J.et.al. 8093236 [8] “Point mutations in a conserved region (TonB box) of Escherichia coli outer membrane protein BtuB affect vitamin B12 transport.” Gudmundsdottir A.et.al. 2687240 [9] “Coupled changes in translation and transcription during cobalamin-dependent regulation of btuB expression in Escherichia coli.” Nou X.et.al. 9852020 [10] “Site-directed disulfide bonding reveals an interaction site between energy-coupling protein TonB and BtuB, the outer membrane cobalamin transporter.” Cadieux N.et.al. 10485884 [11] “Transport-defective mutations alter the conformation of the energy-coupling motif of an outer membrane transporter.” Coggshall K.A.et.al. 11705387 [12] “The Escherichia coli outer membrane cobalamin transporter BtuB: structural analysis of calcium and substrate binding, and identification of orthologous transporters by sequence/structure conservation.” Chimento D.P.et.al. 14499604 [13] “Crystallization and initial X-ray diffraction of BtuB, the integral membrane cobalamin transporter of Escherichia coli.” Chimento D.P.et.al. 12595710 | |
Structure: | |
[...more] |
External Searches:
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Analyze:
Predict TMSs (Predict number of transmembrane segments) | ||||
FASTA formatted sequence |
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1: MIKKASLLTA CSVTAFSAWA QDTSPDTLVV TANRFEQPRS TVLAPTTVVT RQDIDRWQST 61: SVNDVLRRLP GVDITQNGGS GQLSSIFIRG TNASHVLVLI DGVRLNLAGV SGSADLSQFP 121: IALVQRVEYI RGPRSAVYGS DAIGGVVNII TTRDEPGTEI SAGWGSNSYQ NYDVSTQQQL 181: GDKTRVTLLG DYAHTHGYDV VAYGNTGTQA QTDNDGFLSK TLYGALEHNF TDAWSGFVRG 241: YGYDNRTNYD AYYSPGSPLL DTRKLYSQSW DAGLRYNGEL IKSQLITSYS HSKDYNYDPH 301: YGRYDSSATL DEMKQYTVQW ANNVIVGHGS IGAGVDWQKQ TTTPGTGYVE DGYDQRNTGI 361: YLTGLQQVGD FTFEGAARSD DNSQFGRHGT WQTSAGWEFI EGYRFIASYG TSYKAPNLGQ 421: LYGFYGNPNL DPEKSKQWEG AFEGLTAGVN WRISGYRNDV SDLIDYDDHT LKYYNEGKAR 481: IKGVEATANF DTGPLTHTVS YDYVDARNAI TDTPLLRRAK QQVKYQLDWQ LYDFDWGITY 541: QYLGTRYDKD YSSYPYQTVK MGGVSLWDLA VAYPVTSHLT VRGKIANLFD KDYETVYGYQ 601: TAGREYTLSG SYTF