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Protein

Phospholipase C

Gene

plc

Organism
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.

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Toxin

Keywords - Biological processi

Cytolysis, Hemolysis

Keywords - Ligandi

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
OrganismiClostridium bifermentans
Taxonomic identifieri1490 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptostreptococcaceaeParaclostridium

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.
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
Contains 1 PLAT domain.PROSITE-ProRule annotation
Contains 1 Zn-dependent PLC domain.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.
InterProiIPR001024. PLAT/LH2_dom.
IPR008947. PLipase_C/P1_nuclease.
IPR029002. PLPC/GPLD1.
IPR001531. Zn_PLipaseC.
[Graphical view]
PfamiPF01477. PLAT. 1 hit.
PF00882. Zn_dep_PLPC. 1 hit.
[Graphical view]
PRINTSiPR00479. PRPHPHLPASEC.
ProDomiPD003946. PLipaseC_Zn-bd_prok. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00770. Zn_dep_PLPC. 1 hit.
[Graphical view]
SUPFAMiSSF48537. SSF48537. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEiPS50095. PLAT. 1 hit.
PS00384. PROKAR_ZN_DEPEND_PLPC_1. 1 hit.
PS51346. PROKAR_ZN_DEPEND_PLPC_2. 1 hit.
[Graphical view]

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.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliP20419.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

CDDicd11009. Zn_dep_PLPC. 1 hit.
Gene3Di1.10.575.10. 1 hit.
2.60.60.20. 1 hit.
InterProiIPR001024. PLAT/LH2_dom.
IPR008947. PLipase_C/P1_nuclease.
IPR029002. PLPC/GPLD1.
IPR001531. Zn_PLipaseC.
[Graphical view]
PfamiPF01477. PLAT. 1 hit.
PF00882. Zn_dep_PLPC. 1 hit.
[Graphical view]
PRINTSiPR00479. PRPHPHLPASEC.
ProDomiPD003946. PLipaseC_Zn-bd_prok. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00770. Zn_dep_PLPC. 1 hit.
[Graphical view]
SUPFAMiSSF48537. SSF48537. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEiPS50095. PLAT. 1 hit.
PS00384. PROKAR_ZN_DEPEND_PLPC_1. 1 hit.
PS51346. PROKAR_ZN_DEPEND_PLPC_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPHLC_CLOBI
AccessioniPrimary (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: October 5, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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.