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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi27 – 271Zinc 1PROSITE-ProRule annotation
Metal bindingi37 – 371Zinc 1PROSITE-ProRule annotation
Metal bindingi82 – 821Zinc 3PROSITE-ProRule annotation
Metal bindingi94 – 941Zinc 3PROSITE-ProRule annotation
Metal bindingi152 – 1521Zinc 3PROSITE-ProRule annotation
Metal bindingi156 – 1561Zinc 1PROSITE-ProRule annotation
Metal bindingi156 – 1561Zinc 3PROSITE-ProRule annotation
Metal bindingi162 – 1621Zinc 2PROSITE-ProRule annotation
Metal bindingi174 – 1741Zinc 2PROSITE-ProRule annotation
Metal bindingi178 – 1781Zinc 2PROSITE-ProRule annotation
Metal bindingi297 – 2971Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi298 – 2981Calcium 3By similarity
Metal bindingi299 – 2991Calcium 3By similarity
Metal bindingi319 – 3191Calcium 2By similarity
Metal bindingi320 – 3201Calcium 2By similarity
Metal bindingi322 – 3221Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi323 – 3231Calcium 3By similarity
Metal bindingi324 – 3241Calcium 2By similarity
Metal bindingi324 – 3241Calcium 3By similarity
Metal bindingi363 – 3631Calcium 1By similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626By similarityAdd
BLAST
Chaini27 – 398372Phospholipase CPRO_0000023933Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP20419.
SMRiP20419. Positions 27-397.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 276250Zn-dependent PLCPROSITE-ProRule annotationAdd
BLAST
Domaini282 – 398117PLATPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni273 – 2819Linker

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

Gene3Di1.10.575.10. 1 hit.
2.60.60.20. 1 hit.
InterProiIPR001024. PLAT/LH2_dom.
IPR008947. PLipase_C/P1_nuclease.
IPR001531. PLipaseC_domain.
IPR029002. PLPC/GPLD1.
[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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti120 – 1234SRNS → AETQ (PubMed:10377104).Curated
Sequence conflicti120 – 1234SRNS → AETQ (PubMed:12540540).Curated
Sequence conflicti272 – 2743GNT → ENI in BAB83265 (PubMed:12540540).Curated
Sequence conflicti280 – 2801L → S in BAB83265 (PubMed:12540540).Curated
Sequence conflicti311 – 3111G → D in BAB83265 (PubMed:12540540).Curated
Sequence conflicti357 – 3571R → K in BAB83265 (PubMed:12540540).Curated

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.
SMRiP20419. Positions 27-397.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di1.10.575.10. 1 hit.
2.60.60.20. 1 hit.
InterProiIPR001024. PLAT/LH2_dom.
IPR008947. PLipase_C/P1_nuclease.
IPR001531. PLipaseC_domain.
IPR029002. PLPC/GPLD1.
[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...

Publicationsi

  1. "Cloning and expression of the phospholipase C gene from Clostridium perfringens and Clostridium bifermentans."
    Tso J.Y., Siebel C.
    Infect. Immun. 57:468-476(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    Strain: ATCC 638 / DSM 14991 / JCM 1386 / NCIMB 10716 / NCTC 13019.
  2. "Differences in the carboxy-terminal (putative phospholipid binding) domains of Clostridium perfringens and Clostridium bifermentans phospholipases C influence the hemolytic and lethal properties of these enzymes."
    Jepson M., Howells A.M., Bullifent H.L., Bolgiano B., Crane D.T., Miller J., Holley J., Jayasekera P., Titball R.W.
    Infect. Immun. 67:3297-3301(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CONSTRUCTION OF A HYBRID ENZYME.
    Strain: ATCC 638 / DSM 14991 / JCM 1386 / NCIMB 10716 / NCTC 13019.
  3. "Clostridium sordellii phospholipase C: gene cloning and comparison of enzymatic and biological activities with those of Clostridium perfringens and Clostridium bifermentans phospholipase C."
    Karasawa T., Wang X., Maegawa T., Michiwa Y., Kita H., Miwa K., Nakamura S.
    Infect. Immun. 71:641-646(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: KZ 1012.
  4. "Structure and function of clostridial phospholipases C."
    Jepson M., Titball R.W.
    Microbes Infect. 2:1277-1284(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

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: July 6, 2016
This is version 106 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.