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3.A.15.2.1
The pilin secretion/fimbrial assembly system. The PilB and PilT ATPases act antagonistically in Type IV pilus function in Myxococcus xanthus. ATP binding and hydrolysis by PilT are essential for T4P extension while ATP binding and hydrolysis by PilB are essential for T4P retraction. Thus, PilB and PilT act at distinct steps in the T4P extension/retraction cycle (Jakovljevic et al., 2008).

Accession Number:P22610
Protein Name:PilD aka XCPA aka PA4528
Length:290
Molecular Weight:31870.00
Species:Pseudomonas aeruginosa [287]
Number of TMSs:6
Location1 / Topology2 / Orientation3: Cell inner membrane1 / Multi-pass membrane protein2
Substrate

Cross database links:

RefSeq: NP_253218.1   
Entrez Gene ID: 877861   
Pfam: PF06750    PF01478   
BioCyc: PAER208964:PA4528-MONOMER   
KEGG: pae:PA4528   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005886 C:plasma membrane
GO:0004190 F:aspartic-type endopeptidase activity
GO:0008168 F:methyltransferase activity

References (7)

[1] “Products of three accessory genes, pilB, pilC, and pilD, are required for biogenesis of Pseudomonas aeruginosa pili.”  Nunn D.et.al.   1971619
[2] “Protein secretion in Pseudomonas aeruginosa: the xcpA gene encodes an integral inner membrane protein homologous to Klebsiella pneumoniae secretion function protein PulO.”  Bally M.et.al.   1898929
[3] “Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen.”  Stover C.K.et.al.   10984043
[4] “Structure-function relationship of type-IV prepilin peptidase of Pseudomonas aeruginosa -- a review.”  Lory S.et.al.   9224881
[5] “Posttranslational processing of type IV prepilin and homologs by PilD of Pseudomonas aeruginosa.”  Strom M.S.et.al.   8057924
[6] “Identification of active-site cysteines in the conserved domain of PilD, the bifunctional type IV pilin leader peptidase/N-methyltransferase of Pseudomonas aeruginosa.”  Strom M.S.et.al.   8340405
[7] “Amino acid substitutions in PilD, a bifunctional enzyme of Pseudomonas aeruginosa. Effect on leader peptidase and N-methyltransferase activities in vitro and in vivo.”  Pepe J.C.et.al.   9668097

External Searches:

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Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
FASTA formatted sequence 
1:	MPLLDYLASH PLAFVLCTIL LGLLVGSFLN VVVHRLPKMM ERNWKAEARE ALGLEPEPKQ 
61:	ATYNLVLPNS ACPRCGHEIR PWENIPLVSY LALGGKCSSC KAAIGKRYPL VELATALLSG 
121:	YVAWHFGFTW QAGAMLLLTW GLLAMSLIDA DHQLLPDVLV LPLLWLGLIA NHFGLFASLD 
181:	DALFGAVFGY LSLWSVFWLF KLVTGKEGMG YGDFKLLAML GAWGGWQILP LTILLSSLVG 
241:	AILGVIMLRL RNAESGTPIP FGPYLAIAGW IALLWGDQIT RTYLQFAGFK