CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013724
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zinc metalloprotease RasP 
Protein Synonyms/Alias
 Regulating alternative sigma factor protease; Regulating anti-sigma-W factor activity protease 
Gene Name
 rasP 
Gene Synonyms/Alias
 GK1256 
Created Date
 July 27, 2013 
Organism
 Geobacillus kaustophilus (strain HTA426) 
NCBI Taxa ID
 235909 
Lysine Modification
Position
Peptide
Type
References
392GKPVDRQKEGMVHFIacetylation[1]
Reference
 [1] Proteomic analysis of acetylation in thermophilic Geobacillus kaustophilus.
 Lee DW, Kim D, Lee YJ, Kim JA, Choi JY, Kang S, Pan JG.
 Proteomics. 2013 Aug;13(15):2278-82. [PMID: 23696451
Functional Description
 Is responsible for Site-2 cleavage of the RsiW anti- sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor (By similarity). 
Sequence Annotation
 DOMAIN 186 271 PDZ.
 ACT_SITE 23 23 Potential.
 METAL 22 22 Zinc; catalytic (Potential).
 METAL 26 26 Zinc; catalytic (Potential).  
Keyword
 Cell membrane; Complete proteome; Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease; Transmembrane; Transmembrane helix; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 421 AA 
Protein Sequence
MVETLESIIS FIVVFGALVF FHELGHLLLA KRAGILCREF AIGFGPKVFS FKKNETVYTI 60
RLLPLGGFVR MAGEDPETIE LKRGQVVGLL LDESGQVEKI VLNHKDDYPN IRVVEVEEAD 120
LEHGMYVTGY TDGERFERFT VKEPAFFVVD RQEIQIAPYH RQFAAKTLGQ RTMTILAGPL 180
ANFLLSLVVF IIIGLLQGYP VDKPVIGELT PEGAARAAGL KQGDKVIAIN GERMETWTEI 240
VNTIRAHPGE PLQFQIERNG KERSVTVTPE AKTVQGETIG LIGVYQPMEK SVLGSIKQGL 300
VETYYWTREI VTGLGQLITG QFQLDMLSGP VGIAVSTGKV AESGIYYLMK WGAILSINLG 360
IVNLLPLPAL DGGRLLFFAI EAVRGKPVDR QKEGMVHFIG FALLMLLMLV VTWNDIQKFF 420
L 421 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR001478; PDZ.
 IPR004387; Pept_M50_Zn.
 IPR008915; Peptidase_M50. 
Pfam
 PF13180; PDZ_2
 PF02163; Peptidase_M50 
SMART
 SM00228; PDZ 
PROSITE
 PS50106; PDZ
 PS00142; ZINC_PROTEASE 
PRINTS