UniProtKB - P20419 (PHLC_PARBF)
(max 400 entries)x
Your basket is currently empty. i
Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)
Protein
Phospholipase C
Gene
plc
Organism
Paraclostridium bifermentans (Clostridium bifermentans)
Status
Functioni
Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture. Binds to eukaryotic membranes where it hydrolyzes phosphatidylcholine. This enzyme has 10-fold less activity towards sphingomyelin than its C.perfringens counterpart, is approximately 100-fold less hemolytic against mouse erythrocytes and at least 100-fold less toxic in mice.
Miscellaneous
A hybrid protein between the N-terminus of C.bifermentans and the C-terminus of C.perfringens has an activity intermediate between the two.
Catalytic activityi
A phosphatidylcholine + H2O = 1,2-diacyl-sn-glycerol + phosphocholine.
Cofactori
Protein has several cofactor binding sites:- Ca2+By similarityNote: Binds 3 Ca2+ ions per subunit.By similarity
- Zn2+PROSITE-ProRule annotationNote: Binds 3 Zn2+ ions per subunit.PROSITE-ProRule annotation
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 27 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 37 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 82 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 94 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 152 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 156 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 156 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 162 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 174 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 178 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 297 | Calcium 1; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 298 | Calcium 3By similarity | 1 | |
Metal bindingi | 299 | Calcium 3By similarity | 1 | |
Metal bindingi | 319 | Calcium 2By similarity | 1 | |
Metal bindingi | 320 | Calcium 2By similarity | 1 | |
Metal bindingi | 322 | Calcium 2; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 323 | Calcium 3By similarity | 1 | |
Metal bindingi | 324 | Calcium 2By similarity | 1 | |
Metal bindingi | 324 | Calcium 3By similarity | 1 | |
Metal bindingi | 363 | Calcium 1By similarity | 1 |
GO - Molecular functioni
- phosphatidylcholine phospholipase C activity Source: UniProtKB-EC
- toxin activity Source: UniProtKB-KW
- zinc ion binding Source: InterPro
GO - Biological processi
- hemolysis in other organism Source: UniProtKB-KW
Keywordsi
Molecular function | Hydrolase, Toxin |
Biological process | Cytolysis, Hemolysis |
Ligand | Calcium, Metal-binding, Zinc |
Names & Taxonomyi
Protein namesi | Recommended name: Phospholipase C (EC:3.1.4.3)Short name: PLC Alternative name(s): Cbp Phosphatidylcholine cholinephosphohydrolase |
Gene namesi | Name:plc Synonyms:cbp |
Organismi | Paraclostridium bifermentans (Clostridium bifermentans) |
Taxonomic identifieri | 1490 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Clostridia › Clostridiales › Peptostreptococcaceae › Paraclostridium |
Subcellular locationi
- Secreted PROSITE-ProRule annotation
GO - Cellular componenti
- extracellular region Source: UniProtKB-SubCell
Keywords - Cellular componenti
SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 26 | By similarityAdd BLAST | 26 | |
ChainiPRO_0000023933 | 27 – 398 | Phospholipase CAdd BLAST | 372 |
Structurei
3D structure databases
ProteinModelPortali | P20419. |
SMRi | P20419. |
ModBasei | Search... |
MobiDBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 27 – 276 | Zn-dependent PLCPROSITE-ProRule annotationAdd BLAST | 250 | |
Domaini | 282 – 398 | PLATPROSITE-ProRule annotationAdd BLAST | 117 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 273 – 281 | Linker | 9 |
Domaini
The protein is composed of 2 domains; the N-terminal domain contains the phospholipase C active site (PLC), in a cleft which is also occupied by the 3 zinc ions. The C-terminal domain is a putative phospholipid-recognition domain, which shows structural homology with phospholipid-binding C2-like domains from a range of eukaryotic proteins. The ability to bind membrane phospholipids in a Ca2+ dependent manner is conferred by this C-terminal domain (By similarity).By similarity
Sequence similaritiesi
Belongs to the bacterial zinc-metallophospholipase C family.PROSITE-ProRule annotation
Keywords - Domaini
SignalFamily and domain databases
CDDi | cd11009. Zn_dep_PLPC. 1 hit. |
Gene3Di | 1.10.575.10. 1 hit. |
InterProi | View protein in InterPro IPR001024. PLAT/LH2_dom. IPR036392. PLAT/LH2_dom_sf. IPR008947. PLipase_C/P1_nuclease_dom_sf. IPR029002. PLPC/GPLD1. IPR001531. Zn_PLipaseC. |
Pfami | View protein in Pfam PF01477. PLAT. 1 hit. PF00882. Zn_dep_PLPC. 1 hit. |
PRINTSi | PR00479. PRPHPHLPASEC. |
ProDomi | View protein in ProDom or Entries sharing at least one domain PD003946. PLipaseC_Zn-bd_prok. 1 hit. |
SMARTi | View protein in SMART SM00770. Zn_dep_PLPC. 1 hit. |
SUPFAMi | SSF48537. SSF48537. 1 hit. SSF49723. SSF49723. 1 hit. |
PROSITEi | View protein in PROSITE PS50095. PLAT. 1 hit. PS00384. PROKAR_ZN_DEPEND_PLPC_1. 1 hit. PS51346. PROKAR_ZN_DEPEND_PLPC_2. 1 hit. |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P20419-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKALKKVSNI LCVLGLCTLM GGTSYAWDGK KDGTGTHSLI AEHGLSMLNN
60 70 80 90 100
DLSGNESQQV KDNIKILNEY LGDLKLGSTY PDYDPNAYDL YQDHFYDPDT
110 120 130 140 150
GNNFTIDNSW YASYPIYDTS RNSVRKFATL AKNEWEKGNF KEATFLLGQG
160 170 180 190 200
LHYLGDLNTP YHASNVTAVD SPGHVKYETF VEERKDNYAL NTSGNDTTSG
210 220 230 240 250
VYKEAMENPS FNKWMTQNSI KYAKIAKDLY YSHSTMSHSW DDWDYSGREA
260 270 280 290 300
IKNSQVCTAG FLYRFMNEVS NGNTGDNDSL TNEFNIVLKT ADNKYAGTDD
310 320 330 340 350
NVYFGFETNE GKKFEWKLDN AGNDFERNQV DNYILKTKDG EEVDINNISN
360 370 380 390
YWIRKERLTS ISDDWELSNF KLIANGKVIQ QQDVNKVFTG NETYYINK
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 120 – 123 | SRNS → AETQ (PubMed:10377104).Curated | 4 | |
Sequence conflicti | 120 – 123 | SRNS → AETQ (PubMed:12540540).Curated | 4 | |
Sequence conflicti | 272 – 274 | GNT → ENI in BAB83265 (PubMed:12540540).Curated | 3 | |
Sequence conflicti | 280 | L → S in BAB83265 (PubMed:12540540).Curated | 1 | |
Sequence conflicti | 311 | G → D in BAB83265 (PubMed:12540540).Curated | 1 | |
Sequence conflicti | 357 | R → K in BAB83265 (PubMed:12540540).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF072123 Genomic DNA. Translation: AAD41623.1. AB061869 Genomic DNA. Translation: BAB83265.1. |
PIRi | B30565. |
Similar proteinsi
Entry informationi
Entry namei | PHLC_PARBF | |
Accessioni | P20419Primary (citable) accession number: P20419 Secondary accession number(s): Q8VUZ4, Q9S532 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1991 |
Last sequence update: | February 1, 1991 | |
Last modified: | March 28, 2018 | |
This is version 114 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |