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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'.

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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi188 – 1881Zinc; catalyticPROSITE-ProRule annotation
Active sitei189 – 1891PROSITE-ProRule annotation
Metal bindingi192 – 1921Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi228 – 2281Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi265 – 2651Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi267 – 2671Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi297 – 2971Calcium 1By similarity
Metal bindingi299 – 2991Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi300 – 3001Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi302 – 3021Calcium 1By similarity
Metal bindingi302 – 3021Calcium 2By similarity
Metal bindingi339 – 3391Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi341 – 3411Calcium 2By similarity
Metal bindingi346 – 3461Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi348 – 3481Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi350 – 3501Calcium 3By similarity
Metal bindingi355 – 3551Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi357 – 3571Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi359 – 3591Calcium 4By similarity
Metal bindingi363 – 3631Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi364 – 3641Calcium 5; via carbonyl oxygenBy similarity
Metal bindingi365 – 3651Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi366 – 3661Calcium 5; via carbonyl oxygenBy similarity
Metal bindingi368 – 3681Calcium 3By similarity
Metal bindingi368 – 3681Calcium 5By similarity
Metal bindingi372 – 3721Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi373 – 3731Calcium 6; via carbonyl oxygenBy similarity
Metal bindingi375 – 3751Calcium 6; via carbonyl oxygenBy similarity
Metal bindingi377 – 3771Calcium 4By similarity
Metal bindingi377 – 3771Calcium 6By similarity
Metal bindingi381 – 3811Calcium 5; via carbonyl oxygenBy similarity
Metal bindingi382 – 3821Calcium 7; via carbonyl oxygenBy similarity
Metal bindingi383 – 3831Calcium 5; via carbonyl oxygenBy similarity
Metal bindingi384 – 3841Calcium 7; via carbonyl oxygenBy similarity
Metal bindingi386 – 3861Calcium 5By similarity
Metal bindingi386 – 3861Calcium 7By similarity
Metal bindingi395 – 3951Calcium 6By similarity
Metal bindingi402 – 4021Calcium 6By similarity
Metal bindingi412 – 4121Calcium 7By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Protein family/group databases

MEROPSiM10.054.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeDickeya

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 1717PRO_0000028689Add
BLAST
Chaini18 – 479462Serralysin CPRO_0000028690Add
BLAST

Keywords - PTMi

Zymogen

Structurei

Secondary structure

1
479
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi22 – 309Combined sources
Turni31 – 344Combined sources
Helixi50 – 578Combined sources
Turni58 – 603Combined sources
Beta strandi66 – 683Combined sources
Beta strandi74 – 807Combined sources
Helixi99 – 11315Combined sources
Beta strandi116 – 1227Combined sources
Beta strandi130 – 1367Combined sources
Beta strandi150 – 1523Combined sources
Beta strandi155 – 1584Combined sources
Turni159 – 1624Combined sources
Beta strandi163 – 1675Combined sources
Helixi171 – 1744Combined sources
Turni176 – 1783Combined sources
Helixi180 – 19314Combined sources
Beta strandi199 – 2013Combined sources
Beta strandi204 – 2074Combined sources
Helixi211 – 2133Combined sources
Turni221 – 2233Combined sources
Beta strandi227 – 2293Combined sources
Helixi231 – 2344Combined sources
Helixi248 – 25811Combined sources
Turni262 – 2654Combined sources
Beta strandi270 – 2723Combined sources
Helixi280 – 2823Combined sources
Beta strandi293 – 2953Combined sources
Beta strandi303 – 3053Combined sources
Beta strandi314 – 3163Combined sources
Beta strandi322 – 3243Combined sources
Beta strandi332 – 3343Combined sources
Beta strandi342 – 3443Combined sources
Beta strandi351 – 3533Combined sources
Beta strandi360 – 3623Combined sources
Beta strandi369 – 3713Combined sources
Beta strandi378 – 3803Combined sources
Beta strandi387 – 3893Combined sources
Helixi393 – 3953Combined sources
Helixi398 – 4003Combined sources
Beta strandi402 – 4043Combined sources
Turni409 – 4113Combined sources
Beta strandi413 – 4153Combined sources
Helixi417 – 4226Combined sources
Beta strandi434 – 4363Combined sources
Beta strandi438 – 4447Combined sources
Turni445 – 4484Combined sources
Beta strandi449 – 4557Combined sources
Beta strandi464 – 4707Combined sources
Helixi474 – 4763Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GO7X-ray2.10P18-479[»]
1GO8X-ray2.00P18-479[»]
1K7GX-ray2.00A1-479[»]
1K7IX-ray1.59A1-479[»]
1K7QX-ray1.80A1-479[»]
3HB2X-ray1.75P18-479[»]
3HBUX-ray1.77P18-479[»]
3HBVX-ray1.95P18-479[»]
3HDAX-ray2.13P18-479[»]
ProteinModelPortaliP16317.
SMRiP16317. Positions 25-479.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16317.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati344 – 36118Hemolysin-type calcium-binding 1Add
BLAST
Repeati362 – 37918Hemolysin-type calcium-binding 2Add
BLAST
Repeati380 – 39718Hemolysin-type calcium-binding 3Add
BLAST

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

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. 3 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.

P16317-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKNLSLRQD DAQHALSANT SSAYNSVYDF LRYHDRGDGL TVNGKTSYSI
60 70 80 90 100
DQAAAQITRE NVSWNGTNVF GKSANLTFKF LQSVSSIPSG DTGFVKFNAE
110 120 130 140 150
QIEQAKLSLQ SWSDVANLTF TEVTGNKSAN ITFGNYTRDA SGNLDYGTQA
160 170 180 190 200
YAYYPGNYQG AGSSWYNYNQ SNIRNPGSEE YGRQTFTHEI GHALGLAHPG
210 220 230 240 250
EYNAGEGDPS YNDAVYAEDS YQFSIMSYWG ENETGADYNG HYGGAPMIDD
260 270 280 290 300
IAAIQRLYGA NMTTRTGDSV YGFNSNTDRD FYTATDSSKA LIFSVWDAGG
310 320 330 340 350
TDTFDFSGYS NNQRINLNEG SFSDVGGLKG NVSIAHGVTI ENAIGGSGND
360 370 380 390 400
ILVGNSADNI LQGGAGNDVL YGGAGADTLY GGAGRDTFVY GSGQDSTVAA
410 420 430 440 450
YDWIADFQKG IDKIDLSAFR NEGQLSFVQD QFTGKGQEVM LQWDAANSIT
460 470
NLWLHEAGHS SVDFLVRIVG QAAQSDIIV
Length:479
Mass (Da):51,601
Last modified:November 1, 1991 - v2
Checksum:i990ED8376725DF61
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59229 Genomic DNA. Translation: AAA24860.1.
J04736 Genomic DNA. Translation: AAA24862.1.
M60395 Genomic DNA. Translation: AAA63638.1.
PIRiA38307.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59229 Genomic DNA. Translation: AAA24860.1.
J04736 Genomic DNA. Translation: AAA24862.1.
M60395 Genomic DNA. Translation: AAA63638.1.
PIRiA38307.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GO7X-ray2.10P18-479[»]
1GO8X-ray2.00P18-479[»]
1K7GX-ray2.00A1-479[»]
1K7IX-ray1.59A1-479[»]
1K7QX-ray1.80A1-479[»]
3HB2X-ray1.75P18-479[»]
3HBUX-ray1.77P18-479[»]
3HBVX-ray1.95P18-479[»]
3HDAX-ray2.13P18-479[»]
ProteinModelPortaliP16317.
SMRiP16317. Positions 25-479.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM10.054.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP16317.

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. 3 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...

Publicationsi

  1. "Protein secretion in Gram-negative bacteria. The extracellular metalloprotease B from Erwinia chrysanthemi contains a C-terminal secretion signal analogous to that of Escherichia coli alpha-hemolysin."
    Delepelaire P., Wandersman C.
    J. Biol. Chem. 265:17118-17125(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: B374.
  2. "Protease secretion by Erwinia chrysanthemi. Proteases B and C are synthesized and secreted as zymogens without a signal peptide."
    Delepelaire P., Wandersman C.
    J. Biol. Chem. 264:9083-9089(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59, PARTIAL PROTEIN SEQUENCE.
    Strain: B374.

Entry informationi

Entry nameiPRTC_DICCH
AccessioniPrimary (citable) accession number: P16317
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: November 1, 1991
Last modified: October 14, 2015
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.