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3.A.1.15.8
Manganese (Mn2+), zinc (Zn2+) and possibly iron (Fe2+) uptake porter, TroABCD (Hazlett et al., 2003).  Transcription of the operon is controlled by the Mn2+-activated (not Zn2+- or Fe2+-activated) repressor, TroR (153 aas, acc# F7IW50;) TroR contains a metal-binding domain homologous to the YtgC-R protein (3.A.1.15.12) which has the membrane domain of this ABC transporter (N-terminus) fused to the repressor domain (C-terminus) (Liu et al. 2013).  TroA (Tromp1), the periplasmic metal binding protein, was originally reported to be an outer membrane porin (Zhang et al. 1999), but this proved to be incorrect.

Accession Number:P96118
Protein Name:TroC
Length:298
Molecular Weight:31540.00
Species:Treponema pallidum [160]
Number of TMSs:7
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate Zn2+, Mn2+, Fe2+

Cross database links:

HEGENOM: HBG733179
RefSeq: NP_218604.1   
Entrez Gene ID: 2611129   
Pfam: PF00950   
BioCyc: TPAL243276:TP_0165-MONOMER   
KEGG: tpa:TP0165   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005886 C:plasma membrane
GO:0005524 F:ATP binding
GO:0042626 F:ATPase activity, coupled to transmembrane m...
GO:0006829 P:zinc ion transport

References (2)

[1] “Identification and transcriptional analysis of a Treponema pallidum operon encoding a putative ABC transport system, an iron-activated repressor protein homolog, and a glycolytic pathway enzyme homolog.”  Hardham J.M.et.al.   9332349
[2] “Complete genome sequence of Treponema pallidum, the syphilis spirochete.”  Fraser C.M.et.al.   9665876

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MHALMRLFSD YTLQNVVLGT LFLGLGSGLV GSFAVLRRQS LFGDAVSHAT LPGIVIAFLL 
61:	TGTKSTEILL LGAALSGLVG TVVMLMVMRT TKIDTDGAQG IVLGVFLGFG FLLLTHVQKS 
121:	PQAAKAGLNK FILGQAATIL QRDVLLIIAM EVVIGLLVLL FWKELKLSTF DRDFSAVQGF 
181:	SPQLMEFMLT ALIVVAVVVG VQAVGVILMS ALLTAPAVAA RQWTNSLRVL CALAALFGGV 
241:	SGVSGSVVSA QVPRLSTGPV IVLVLTGIAL VSIMLGPQRG VLYQLWRRRR VSLLQEEG