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2.A.15.1.4 The high-affinity, proton- or sodium-driven, secondary symporter, BetT. The cytoplasmic C-terminal domain of plays a role in the regulation of BetT activity; C-terminal truncations cause BetT to be permanently locked in a low-transport-activity mode. (Tøndervik and Strøm 2007).
Accession Number:	P0ABC9
Protein Name:	High-affinity choline transport protein BetT aka B0314
Length:	677
Molecular Weight:	75842.00
Species:	Escherichia coli [83333]
Number of TMSs:	12
Location¹ / Topology² / Orientation³:	Cell inner membrane¹ / Multi-pass membrane protein²
Substrate	sodium(1+), choline

RefSeq:	AP_000967.1 NP_414848.1
Entrez Gene ID:	945079
Pfam:	PF02028
BioCyc:	EcoCyc:BETT-MONOMER ECOL168927:B0314-MONOMER
KEGG:	ecj:JW0306 eco:b0314 ecj:JW0306 eco:b0314
Gene Ontology GO:0016021 C:integral to membrane GO:0005886 C:plasma membrane GO:0005215 F:transporter activity GO:0006950 P:response to stress GO:0006810 P:transport
References (8) [1] “DNA sequence and analysis of the bet genes encoding the osmoregulatory choline-glycine betaine pathway of Escherichia coli.” Lamark T.et.al. 1956285 [2] “The complete genome sequence of Escherichia coli K-12.” Blattner F.R.et.al. 9278503 [3] “Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.” Hayashi K.et.al. 16738553 [4] “Global topology analysis of the Escherichia coli inner membrane proteome.” Daley D.O.et.al. 15919996 [5] “DNA sequence and analysis of the bet genes encoding the osmoregulatory choline-glycine betaine pathway of Escherichia coli.” Lamark T.et.al. 1956285 [6] “The complete genome sequence of Escherichia coli K-12.” Blattner F.R.et.al. 9278503 [7] “Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.” Hayashi K.et.al. 16738553 [8] “Global topology analysis of the Escherichia coli inner membrane proteome.” Daley D.O.et.al. 15919996

UniProt (Universal Protein Resource)
CDD Search (Conserved Domain Database)

Predict TMSs (Predict number of transmembrane segments)

FASTA formatted sequence

1:	MTDLSHSREK DKINPVVFYT SAGLILLFSL TTILFRDFSA LWIGRTLDWV SKTFGWYYLL 
61:	AATLYIVFVV CIACSRFGSV KLGPEQSKPE FSLLSWAAML FAAGIGIDLM FFSVAEPVTQ 
121:	YMQPPEGAGQ TIEAARQAMV WTLFHYGLTG WSMYALMGMA LGYFSYRYNL PLTIRSALYP 
181:	IFGKRINGPI GHSVDIAAVI GTIFGIATTL GIGVVQLNYG LSVLFDIPDS MAAKAALIAL 
241:	SVIIATISVT SGVDKGIRVL SELNVALALG LILFVLFMGD TSFLLNALVL NVGDYVNRFM 
301:	GMTLNSFAFD RPVEWMNNWT LFFWAWWVAW SPFVGLFLAR ISRGRTIRQF VLGTLIIPFT 
361:	FTLLWLSVFG NSALYEIIHG GAAFAEEAMV HPERGFYSLL AQYPAFTFSA SVATITGLLF 
421:	YVTSADSGAL VLGNFTSQLK DINSDAPGWL RVFWSVAIGL LTLGMLMTNG ISALQNTTVI 
481:	MGLPFSFVIF FVMAGLYKSL KVEDYRRESA NRDTAPRPLG LQDRLSWKKR LSRLMNYPGT 
541:	RYTKQMMETV CYPAMEEVAQ ELRLRGAYVE LKSLPPEEGQ QLGHLDLLVH MGEEQNFVYQ 
601:	IWPQQYSVPG FTYRARSGKS TYYRLETFLL EGSQGNDLMD YSKEQVITDI LDQYERHLNF 
661:	IHLHREAPGH SVMFPDA

2.A.15.1.4
The high-affinity, proton- or sodium-driven, secondary symporter, BetT. The cytoplasmic C-terminal domain of plays a role in the regulation of BetT activity; C-terminal truncations cause BetT to be permanently locked in a low-transport-activity mode. (Tøndervik and Strøm 2007).

Cross database links:

Gene Ontology

References (8)

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2.A.15.1.4The high-affinity, proton- or sodium-driven, secondary symporter, BetT. The cytoplasmic C-terminal domain of plays a role in the regulation of BetT activity; C-terminal truncations cause BetT to be permanently locked in a low-transport-activity mode. (Tøndervik and Strøm 2007).

Cross database links:

Gene Ontology

References (8)

External Searches:

Analyze:

2.A.15.1.4
The high-affinity, proton- or sodium-driven, secondary symporter, BetT. The cytoplasmic C-terminal domain of plays a role in the regulation of BetT activity; C-terminal truncations cause BetT to be permanently locked in a low-transport-activity mode. (Tøndervik and Strøm 2007).