Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P20419 (PHLC_PARBF)

(max 400 entries)x

Your basket is currently empty.

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
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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 keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi27Zinc 1PROSITE-ProRule annotation1
Metal bindingi37Zinc 1PROSITE-ProRule annotation1
Metal bindingi82Zinc 3PROSITE-ProRule annotation1
Metal bindingi94Zinc 3PROSITE-ProRule annotation1
Metal bindingi152Zinc 3PROSITE-ProRule annotation1
Metal bindingi156Zinc 1PROSITE-ProRule annotation1
Metal bindingi156Zinc 3PROSITE-ProRule annotation1
Metal bindingi162Zinc 2PROSITE-ProRule annotation1
Metal bindingi174Zinc 2PROSITE-ProRule annotation1
Metal bindingi178Zinc 2PROSITE-ProRule annotation1
Metal bindingi297Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi298Calcium 3By similarity1
Metal bindingi299Calcium 3By similarity1
Metal bindingi319Calcium 2By similarity1
Metal bindingi320Calcium 2By similarity1
Metal bindingi322Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi323Calcium 3By similarity1
Metal bindingi324Calcium 2By similarity1
Metal bindingi324Calcium 3By similarity1
Metal bindingi363Calcium 1By similarity1

GO - Molecular functioni

Complete GO annotation...

GO - Biological processi

Complete GO annotation...

Keywordsi

Molecular functionHydrolase, Toxin
Biological processCytolysis, Hemolysis
LigandCalcium, 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
OrganismiParaclostridium bifermentans (Clostridium bifermentans)
Taxonomic identifieri1490 [NCBI]
Taxonomic lineageiBacteria › Firmicutes › Clostridia › Clostridiales › Peptostreptococcaceae › Paraclostridium

Subcellular locationi

  • Secreted PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26By similarityAdd BLAST26
ChainiPRO_000002393327 – 398Phospholipase CAdd BLAST372

Structurei

3D structure databases

ProteinModelPortaliP20419.
SMRiP20419.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 276Zn-dependent PLCPROSITE-ProRule annotationAdd BLAST250
Domaini282 – 398PLATPROSITE-ProRule annotationAdd BLAST117

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni273 – 281Linker9

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

Signal

Family and domain databases

CDDicd11009. Zn_dep_PLPC. 1 hit.
Gene3Di1.10.575.10. 1 hit.
2.60.60.20. 1 hit.
InterProiView protein in InterPro
IPR001024. PLAT/LH2_dom.
IPR008947. PLipase_C/P1_nuclease.
IPR029002. PLPC/GPLD1.
IPR001531. Zn_PLipaseC.
PfamiView protein in Pfam
PF01477. PLAT. 1 hit.
PF00882. Zn_dep_PLPC. 1 hit.
PRINTSiPR00479. PRPHPHLPASEC.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD003946. PLipaseC_Zn-bd_prok. 1 hit.
SMARTiView protein in SMART
SM00770. Zn_dep_PLPC. 1 hit.
SUPFAMiSSF48537. SSF48537. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEiView protein in PROSITE
PS50095. PLAT. 1 hit.
PS00384. PROKAR_ZN_DEPEND_PLPC_1. 1 hit.
PS51346. PROKAR_ZN_DEPEND_PLPC_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P20419-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:398
Mass (Da):45,366
Last modified:February 1, 1991 - v1
Checksum:i0B628AFE7146BC56
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti120 – 123SRNS → AETQ (PubMed:10377104).Curated4
Sequence conflicti120 – 123SRNS → AETQ (PubMed:12540540).Curated4
Sequence conflicti272 – 274GNT → ENI in BAB83265 (PubMed:12540540).Curated3
Sequence conflicti280L → S in BAB83265 (PubMed:12540540).Curated1
Sequence conflicti311G → D in BAB83265 (PubMed:12540540).Curated1
Sequence conflicti357R → K in BAB83265 (PubMed:12540540).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF072123 Genomic DNA. Translation: AAD41623.1.
AB061869 Genomic DNA. Translation: BAB83265.1.
PIRiB30565.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiPHLC_PARBF
AccessioniPrimary (citable) accession number: P20419
Secondary accession number(s): Q8VUZ4, Q9S532
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: May 10, 2017
This is version 111 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families