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.
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| Accession Number: | P96117 |
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| Protein Name: | TroB |
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| Length: | 266 |
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| Molecular Weight: | 29360.00 |
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| Species: | Treponema pallidum [160] |
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| Number of TMSs: | 1 |
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| Location1 / Topology2 / Orientation3: |
Periplasm1 |
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| Substrate |
iron(2+), zinc(2+), manganese(2+) |
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| RefSeq: |
NP_218603.1
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| Entrez Gene ID: |
2611123
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| Pfam: |
PF00005
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| BioCyc: |
TPAL243276:TP_0164-MONOMER
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| KEGG: |
tpa:TP0164
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[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
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1: MAEISATAYA VQVDDLTLAY RQKPVLWDVD VRIPEGVIEA IIGPNGAGKS TLLKAIMGLL
61: PLASGEVRVF GRPFSKERRR VAYVPQRSAV DWDFPTTVFD VVLMGSYGSL GWILRPGKRE
121: KARAREAIEE VGMGAFLDRQ ISELSGGQQQ RVFLARALVQ DADLYFMDEP FQGVDAATEQ
181: AIVTLLKTLK GRGKTLLVVH HDLQTVAEYF DRVLLLNVRV IAEGAVVSAF TEEYVQRAYG
241: GRISSTLFPR GNKEDVHDAR AHASVL