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Protein

Serralysin C

Gene

prtC

Organism
Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Preferential cleavage of bonds with hydrophobic residues in P1'.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • Ca2+By similarityNote: Binds 7 Ca2+ ions per subunit.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi187Zinc; catalyticPROSITE-ProRule annotation1
Active sitei188PROSITE-ProRule annotation1
Metal bindingi191Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi227Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi264Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi266Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi296Calcium 1By similarity1
Metal bindingi298Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi299Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi301Calcium 1By similarity1
Metal bindingi301Calcium 2By similarity1
Metal bindingi338Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi340Calcium 2By similarity1
Metal bindingi345Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi347Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi349Calcium 3By similarity1
Metal bindingi354Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi356Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi358Calcium 4By similarity1
Metal bindingi362Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi363Calcium 5; via carbonyl oxygenBy similarity1
Metal bindingi364Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi365Calcium 5; via carbonyl oxygenBy similarity1
Metal bindingi367Calcium 3By similarity1
Metal bindingi367Calcium 5By similarity1
Metal bindingi371Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi372Calcium 6; via carbonyl oxygenBy similarity1
Metal bindingi374Calcium 6; via carbonyl oxygenBy similarity1
Metal bindingi376Calcium 4By similarity1
Metal bindingi376Calcium 6By similarity1
Metal bindingi380Calcium 5; via carbonyl oxygenBy similarity1
Metal bindingi381Calcium 7; via carbonyl oxygenBy similarity1
Metal bindingi383Calcium 7; via carbonyl oxygenBy similarity1
Metal bindingi385Calcium 5By similarity1
Metal bindingi385Calcium 7By similarity1
Metal bindingi394Calcium 6By similarity1
Metal bindingi401Calcium 6By similarity1
Metal bindingi411Calcium 7By similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Protein family/group databases

MEROPSiM10.052.

Names & Taxonomyi

Protein namesi
Recommended name:
Serralysin C (EC:3.4.24.40)
Alternative name(s):
Secreted protease C
Short name:
ProC
Gene namesi
Name:prtC
OrganismiDickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi)
Taxonomic identifieri556 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesPectobacteriaceaeDickeya

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000286851 – 17CuratedAdd BLAST17
ChainiPRO_000002868618 – 478Serralysin CAdd BLAST461

Keywords - PTMi

Zymogen

Structurei

3D structure databases

ProteinModelPortaliP19144.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati343 – 360Hemolysin-type calcium-binding 1Add BLAST18
Repeati361 – 378Hemolysin-type calcium-binding 2Add BLAST18

Domaini

The Gly-rich repeats may be important in the extracellular secretion of this metalloprotease.

Sequence similaritiesi

Belongs to the peptidase M10B family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

KOiK01406.

Family and domain databases

Gene3Di2.150.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR018511. Hemolysin-typ_Ca-bd_CS.
IPR001343. Hemolysn_Ca-bd.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR016294. Pept_M10B.
IPR013858. Peptidase_M10B_C.
IPR006026. Peptidase_Metallo.
IPR011049. Serralysin-like_metalloprot_C.
[Graphical view]
PfamiPF00353. HemolysinCabind. 2 hits.
PF00413. Peptidase_M10. 1 hit.
PF08548. Peptidase_M10_C. 1 hit.
[Graphical view]
PIRSFiPIRSF001205. Peptidase_M10B. 1 hit.
SMARTiSM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF51120. SSF51120. 1 hit.
PROSITEiPS00330. HEMOLYSIN_CALCIUM. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P19144-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKNLSSRDD DALHSLSAPS SSYNSIYDLL HYHERGNGLT INGKPSYSIE
60 70 80 90 100
DAGDQITRDN VSWNGANVFG KSANLTFKFL QSARSTPDGD TGFVKFNAAQ
110 120 130 140 150
ISQAKLALQS WADVANVTFT EVTGNQSANV TFGNYTRDSS GRLDYGTQAY
160 170 180 190 200
AYLPGSGSAS GTTWYNYNVD NIRSPDTMEY GRQTLTHEIG HALGLNHPGD
210 220 230 240 250
YNAGEGNPSY SDVTYAEDTR QFSIMSYWSE KNTGGDFKGH YAAGPMLDDI
260 270 280 290 300
AAIQRLYGAN MTTRTGDSVY GFNSNTDRDF YTATSSSKAL IFSAWDAGGN
310 320 330 340 350
DTFDFSGYSN NQRINLNDGS LSDVGGLKGN VSIAEGVTIE NAIGGSGNDL
360 370 380 390 400
LIGNNADNTL RGGAGDDVLF GGSGADRLYG GSGRDTFVYT AASDSKVAAP
410 420 430 440 450
DWLLDFQTGA DKIDLSALNT GNNLHFVNQF SGSGGEIMLN WDASANTSNL
460 470
YLNLDNNTSP EFLVKIVGQV SQTADFVV
Length:478
Mass (Da):51,148
Last modified:November 1, 1990 - v1
Checksum:i91CEFBB8AE7B8598
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M37390 Genomic DNA. Translation: AAA24859.1.
PIRiA36137.

Genome annotation databases

KEGGiag:AAA24859.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M37390 Genomic DNA. Translation: AAA24859.1.
PIRiA36137.

3D structure databases

ProteinModelPortaliP19144.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM10.052.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAA24859.

Phylogenomic databases

KOiK01406.

Family and domain databases

Gene3Di2.150.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR018511. Hemolysin-typ_Ca-bd_CS.
IPR001343. Hemolysn_Ca-bd.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR016294. Pept_M10B.
IPR013858. Peptidase_M10B_C.
IPR006026. Peptidase_Metallo.
IPR011049. Serralysin-like_metalloprot_C.
[Graphical view]
PfamiPF00353. HemolysinCabind. 2 hits.
PF00413. Peptidase_M10. 1 hit.
PF08548. Peptidase_M10_C. 1 hit.
[Graphical view]
PIRSFiPIRSF001205. Peptidase_M10B. 1 hit.
SMARTiSM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF51120. SSF51120. 1 hit.
PROSITEiPS00330. HEMOLYSIN_CALCIUM. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPRTX_DICCH
AccessioniPrimary (citable) accession number: P19144
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: November 2, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Could be the homolog of prtA from strain B374.

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.