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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)DescriptionActionsGraphical viewLength
Metal bindingi188Zinc; catalyticPROSITE-ProRule annotation1
Active sitei189PROSITE-ProRule annotation1
Metal bindingi192Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi228Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi265Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi267Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi297Calcium 1By similarity1
Metal bindingi299Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi300Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi302Calcium 1By similarity1
Metal bindingi302Calcium 2By similarity1
Metal bindingi339Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi341Calcium 2By similarity1
Metal bindingi346Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi348Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi350Calcium 3By similarity1
Metal bindingi355Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi357Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi359Calcium 4By similarity1
Metal bindingi363Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi364Calcium 5; via carbonyl oxygenBy similarity1
Metal bindingi365Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi366Calcium 5; via carbonyl oxygenBy similarity1
Metal bindingi368Calcium 3By similarity1
Metal bindingi368Calcium 5By similarity1
Metal bindingi372Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi373Calcium 6; via carbonyl oxygenBy similarity1
Metal bindingi375Calcium 6; via carbonyl oxygenBy similarity1
Metal bindingi377Calcium 4By similarity1
Metal bindingi377Calcium 6By similarity1
Metal bindingi381Calcium 5; via carbonyl oxygenBy similarity1
Metal bindingi382Calcium 7; via carbonyl oxygenBy similarity1
Metal bindingi383Calcium 5; via carbonyl oxygenBy similarity1
Metal bindingi384Calcium 7; via carbonyl oxygenBy similarity1
Metal bindingi386Calcium 5By similarity1
Metal bindingi386Calcium 7By similarity1
Metal bindingi395Calcium 6By similarity1
Metal bindingi402Calcium 6By similarity1
Metal bindingi412Calcium 7By similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Protein family/group databases

MEROPSiM10.054.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesPectobacteriaceaeDickeya

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000286891 – 17Add BLAST17
ChainiPRO_000002869018 – 479Serralysin CAdd BLAST462

Keywords - PTMi

Zymogen

Structurei

Secondary structure

1479
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi22 – 30Combined sources9
Turni31 – 34Combined sources4
Helixi50 – 57Combined sources8
Turni58 – 60Combined sources3
Beta strandi66 – 68Combined sources3
Beta strandi74 – 80Combined sources7
Helixi99 – 113Combined sources15
Beta strandi116 – 122Combined sources7
Beta strandi130 – 136Combined sources7
Beta strandi150 – 152Combined sources3
Beta strandi155 – 158Combined sources4
Turni159 – 162Combined sources4
Beta strandi163 – 167Combined sources5
Helixi171 – 174Combined sources4
Turni176 – 178Combined sources3
Helixi180 – 193Combined sources14
Beta strandi199 – 201Combined sources3
Beta strandi204 – 207Combined sources4
Helixi211 – 213Combined sources3
Turni221 – 223Combined sources3
Beta strandi227 – 229Combined sources3
Helixi231 – 234Combined sources4
Helixi248 – 258Combined sources11
Turni262 – 265Combined sources4
Beta strandi270 – 272Combined sources3
Helixi280 – 282Combined sources3
Beta strandi293 – 295Combined sources3
Beta strandi303 – 305Combined sources3
Beta strandi314 – 316Combined sources3
Beta strandi322 – 324Combined sources3
Beta strandi332 – 334Combined sources3
Beta strandi342 – 344Combined sources3
Beta strandi351 – 353Combined sources3
Beta strandi360 – 362Combined sources3
Beta strandi369 – 371Combined sources3
Beta strandi378 – 380Combined sources3
Beta strandi387 – 389Combined sources3
Helixi393 – 395Combined sources3
Helixi398 – 400Combined sources3
Beta strandi402 – 404Combined sources3
Turni409 – 411Combined sources3
Beta strandi413 – 415Combined sources3
Helixi417 – 422Combined sources6
Beta strandi434 – 436Combined sources3
Beta strandi438 – 444Combined sources7
Turni445 – 448Combined sources4
Beta strandi449 – 455Combined sources7
Beta strandi464 – 470Combined sources7
Helixi474 – 476Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16317.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati344 – 361Hemolysin-type calcium-binding 1Add BLAST18
Repeati362 – 379Hemolysin-type calcium-binding 2Add BLAST18
Repeati380 – 397Hemolysin-type calcium-binding 3Add 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

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
PDB 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.
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...

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: November 2, 2016
This is version 106 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.