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2.A.6.5.3 The putative glycopeptidolipid exporter, TmtpC (most similar to MmpL of M. leprae; implicated in sliding motility). May function with the MmpS4 protein of Mucobacterium smegmatis (A0QPN7) to form a scaffold for coupled biosynthesis and transport (Deshayes et al., 2010).
Accession Number:	Q9KH53
Protein Name:	TmtpC
Length:	994
Molecular Weight:	107590.00
Species:	Mycobacterium smegmatis [1772]
Number of TMSs:	12
Location¹ / Topology² / Orientation³:	Cell membrane¹ / Multi-pass membrane protein²
Substrate	glycopeptidolipid

Gene Ontology GO:0016021 C:integral to membrane
References (1) [1] “Genetic analysis of sliding motility in Mycobacterium smegmatis.” Recht J.et.al. 10894747

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

Predict TMSs (Predict number of transmembrane segments)

FASTA formatted sequence

1:	MSTEQSGTEK ARRPFFARAV RTLSPFIIVG WLAVILVTTL AAVGGDWSAA IPALERVGEK 
61:	NSVSLMPQDA PSAKAMKHMG QKFEESDSDS FAMIVLEGQE PLGPDALDYY TGLISELRND 
121:	SKHVEHVQDL WGDRLTASSA QSADGKAAYV QLNLAGNQGT PLGDESVAAV RDLVARTPAP 
181:	EGVSVYVTGA APLVSDMQHS GNRSILKITA VTVVIIFAML LMVYRSVITV ILLLIMVGFE 
241:	VAAARGIVAF LGANEVFVLS TFAVNMLVFL AIAAGTDYGI FFFGRYQEAR AAGEDRETAY 
301:	YSMYRGVTPV VMASGLTIAG AIFCLTFTRL PYFHTMGVPC AIGMLAAVAV AVTLVPAGVA 
361:	LAGRIGWLEP KRKMRVRRWR GIGTAIVRWP APILVASLAV ALVGLLALPG YETSYNDRDY 
421:	IPADIPANAG FAAADRHFSQ ARMTPDILMV ESDHDMRNPT DFLVLNKIAK AIFKVRGVSR 
481:	VQGITRPEGT PIERTSIPFL LSLQSAGQVQ ATNFQKQRIG DMLKQVDDMN MMIGVMKTTY 
541:	GVLQELAATT HSLNGSTHEL RDVARDLRGS IAIFDDLLRP IRNYFYWEPH CYNIPICWSL 
601:	RSIFDAMDGV DRLNDELQVL VDNMDRLDAL VPELVAQFPE YIASMETFRE LTLTSYSTFS 
661:	GLLQQMDEQT EDVTAMGQAF DAAKNDDTFF LPPEVFDNPD FKRAMTSFLS PDGKAARFII 
721:	SHNGDPATPE GISRVDQMQT AAVEALKGTP LTDAQVYLAG TAPTAKDWKD GSTYDLLIAG 
781:	IAAMCLIFII MLIVTRSFIA ALVIVGTVVL SLGASFGLSV LLWQYILGIH LHWMVLAMSV 
841:	IILLAVGSDY NLLLVSRIKE EVGAGINTGI VRAMGGTGKV VTSAGLVFAG TMAAMVVSDL 
901:	RIIGQIGTTI GLGLLFDTMI VRSFMTPSIA ALLGRWFWWP QKVRPRPASA LLEPYGPRPL 
961:	VRALLEGPSG AASPGGPGGR LSDDDTPTGP MRTR

2.A.6.5.3
The putative glycopeptidolipid exporter, TmtpC (most similar to MmpL of M. leprae; implicated in sliding motility). May function with the MmpS4 protein of Mucobacterium smegmatis (A0QPN7) to form a scaffold for coupled biosynthesis and transport (Deshayes et al., 2010).

Cross database links:

Gene Ontology

References (1)

External Searches:

Analyze:

2.A.6.5.3The putative glycopeptidolipid exporter, TmtpC (most similar to MmpL of M. leprae; implicated in sliding motility). May function with the MmpS4 protein of Mucobacterium smegmatis (A0QPN7) to form a scaffold for coupled biosynthesis and transport (Deshayes et al., 2010).

Cross database links:

Gene Ontology

References (1)

External Searches:

Analyze:

2.A.6.5.3
The putative glycopeptidolipid exporter, TmtpC (most similar to MmpL of M. leprae; implicated in sliding motility). May function with the MmpS4 protein of Mucobacterium smegmatis (A0QPN7) to form a scaffold for coupled biosynthesis and transport (Deshayes et al., 2010).