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2.A.21.2.1
Proline:Na+ symporter, PutP (Jung et al., 2012).  Extracellular loop 4 (eL4) controls periplasmic entry of substrate to the binding site (Raba et al. 2014).  Interactions between the tip of eL4 and the peptide backbone at the end of TMS 10 participate in coordinating conformational alterations underlying the alternating access mechanism of transport (Bracher et al. 2016).  TMS 6 plays a central role in substrate (both Na+ and proline) binding and release on the inner side of the membrane, and functionally relevant amino acids have been identified (Bracher et al. 2016).

Accession Number:P07117
Protein Name:PutP aka B1015
Length:502
Molecular Weight:54344.00
Species:Escherichia coli [83333]
Number of TMSs:13
Location1 / Topology2 / Orientation3: Cell inner membrane1 / Multi-pass membrane protein2
Substrate proline

Cross database links:

RefSeq: AP_001646.1    NP_415535.1   
Entrez Gene ID: 945602   
Pfam: PF00474   
BioCyc: EcoCyc:PUTP-MONOMER    ECOL168927:B1015-MONOMER   
KEGG: ecj:JW1001    eco:b1015   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005886 C:plasma membrane
GO:0005298 F:proline:sodium symporter activity
GO:0031402 F:sodium ion binding
GO:0015292 F:uniporter activity
GO:0015824 P:proline transport
GO:0006814 P:sodium ion transport
GO:0055085 P:transmembrane transport

References (12)

[1] “Nucleotide sequence of putP, the proline carrier gene of Escherichia coli K12.”  Nakao T.et.al.   3302614
[2] “A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map.”  Oshima T.et.al.   8905232
[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] “Evolutionary genetics of the proline permease gene (putP) and the control region of the proline utilization operon in populations of Salmonella and Escherichia coli.”  Nelson K.et.al.   1400239
[6] “Nucleotide sequence of putC, the regulatory region for the put regulon of Escherichia coli K12.”  Nakao T.et.al.   3325781
[7] “Site-specific alteration of cysteine 281, cysteine 344, and cysteine 349 in the proline carrier of Escherichia coli.”  Yamato I.et.al.   3053687
[8] “Proline carrier mutant of Escherichia coli K-12 with altered cation sensitivity of substrate-binding activity: cloning, biochemical characterization, and identification of the mutation.”  Ohsawa M.et.al.   3053649
[9] “Sodium ion and proline binding sites in the Na+/proline symport carrier of Escherichia coli.”  Hanada K.et.al.   1567896
[10] “Site-specific alteration of arginine 376, the unique positively charged amino acid residue in the mid-membrane-spanning regions of the proline carrier of Escherichia coli.”  Yamato I.et.al.   8119910
[11] “Protein complexes of the Escherichia coli cell envelope.”  Stenberg F.et.al.   16079137
[12] “Global topology analysis of the Escherichia coli inner membrane proteome.”  Daley D.O.et.al.   15919996

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence 
1:	MAISTPMLVT FCVYIFGMIL IGFIAWRSTK NFDDYILGGR SLGPFVTALS AGASDMSGWL 
61:	LMGLPGAVFL SGISESWIAI GLTLGAWINW KLVAGRLRVH TEYNNNALTL PDYFTGRFED 
121:	KSRILRIISA LVILLFFTIY CASGIVAGAR LFESTFGMSY ETALWAGAAA TILYTFIGGF 
181:	LAVSWTDTVQ ASLMIFALIL TPVIVIISVG GFGDSLEVIK QKSIENVDML KGLNFVAIIS 
241:	LMGWGLGYFG QPHILARFMA ADSHHSIVHA RRISMTWMIL CLAGAVAVGF FGIAYFNDHP 
301:	ALAGAVNQNA ERVFIELAQI LFNPWIAGIL LSAILAAVMS TLSCQLLVCS SAITEDLYKA 
361:	FLRKHASQKE LVWVGRVMVL VVALVAIALA ANPENRVLGL VSYAWAGFGA AFGPVVLFSV 
421:	MWSRMTRNGA LAGMIIGALT VIVWKQFGWL GLYEIIPGFI FGSIGIVVFS LLGKAPSAAM 
481:	QKRFAEADAH YHSAPPSRLQ ES