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Protein

Serralysin

Gene

aprA

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: Annotation score: 5 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+Note: Binds 8 Ca2+ ions per subunit.
  • Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi185 – 1851Zinc; via tele nitrogen; catalytic
Active sitei186 – 1861
Metal bindingi189 – 1891Zinc; via tele nitrogen; catalytic
Metal bindingi195 – 1951Zinc; via tele nitrogen; catalytic
Metal bindingi262 – 2621Calcium 1; via carbonyl oxygen
Metal bindingi264 – 2641Calcium 1; via carbonyl oxygen
Metal bindingi266 – 2661Calcium 1
Metal bindingi294 – 2941Calcium 1
Metal bindingi296 – 2961Calcium 1; via carbonyl oxygen
Metal bindingi297 – 2971Calcium 2; via carbonyl oxygen
Metal bindingi299 – 2991Calcium 1
Metal bindingi299 – 2991Calcium 2
Metal bindingi336 – 3361Calcium 2; via carbonyl oxygen
Metal bindingi338 – 3381Calcium 2
Metal bindingi343 – 3431Calcium 3; via carbonyl oxygen
Metal bindingi345 – 3451Calcium 3; via carbonyl oxygen
Metal bindingi347 – 3471Calcium 3
Metal bindingi352 – 3521Calcium 4; via carbonyl oxygen
Metal bindingi354 – 3541Calcium 4; via carbonyl oxygen
Metal bindingi356 – 3561Calcium 4
Metal bindingi360 – 3601Calcium 3; via carbonyl oxygen
Metal bindingi361 – 3611Calcium 5; via carbonyl oxygen
Metal bindingi362 – 3621Calcium 3; via carbonyl oxygen
Metal bindingi363 – 3631Calcium 5; via carbonyl oxygen
Metal bindingi365 – 3651Calcium 3
Metal bindingi365 – 3651Calcium 5
Metal bindingi369 – 3691Calcium 4; via carbonyl oxygen
Metal bindingi370 – 3701Calcium 6; via carbonyl oxygen
Metal bindingi371 – 3711Calcium 4; via carbonyl oxygen
Metal bindingi372 – 3721Calcium 6; via carbonyl oxygen
Metal bindingi374 – 3741Calcium 4
Metal bindingi374 – 3741Calcium 6
Metal bindingi378 – 3781Calcium 5; via carbonyl oxygen
Metal bindingi379 – 3791Calcium 7; via carbonyl oxygen
Metal bindingi380 – 3801Calcium 5; via carbonyl oxygen
Metal bindingi381 – 3811Calcium 7; via carbonyl oxygen
Metal bindingi383 – 3831Calcium 5
Metal bindingi383 – 3831Calcium 7
Metal bindingi392 – 3921Calcium 6; via carbonyl oxygen
Metal bindingi399 – 3991Calcium 6
Metal bindingi409 – 4091Calcium 7
Metal bindingi455 – 4551Calcium 8
Metal bindingi457 – 4571Calcium 8
Metal bindingi459 – 4591Calcium 8
Metal bindingi461 – 4611Calcium 8; via carbonyl oxygen
Metal bindingi463 – 4631Calcium 8

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • metalloendopeptidase activity Source: InterPro
  • peptidase activity Source: PseudoCAP
  • zinc ion binding Source: InterPro

GO - Biological processi

  • negative regulation of complement activation, classical pathway Source: PseudoCAP
  • negative regulation of complement activation, lectin pathway Source: PseudoCAP
  • pathogenesis Source: PseudoCAP
  • positive regulation of sodium ion transport Source: PseudoCAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.40. 5087.

Protein family/group databases

MEROPSiM10.056.

Names & Taxonomyi

Protein namesi
Recommended name:
Serralysin (EC:3.4.24.40)
Alternative name(s):
Alkaline metalloproteinase
Short name:
AP
Gene namesi
Name:aprA
Ordered Locus Names:PA1249
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA1249.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 99PRO_0000028681
Chaini10 – 479470SerralysinPRO_0000028682Add
BLAST

Keywords - PTMi

Zymogen

Proteomic databases

PaxDbiQ03023.

Interactioni

Protein-protein interaction databases

MINTiMINT-204154.
STRINGi208964.PA1249.

Structurei

Secondary structure

1
479
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 2210Combined sources
Turni23 – 253Combined sources
Beta strandi29 – 335Combined sources
Helixi41 – 488Combined sources
Turni49 – 513Combined sources
Beta strandi62 – 709Combined sources
Helixi76 – 794Combined sources
Helixi81 – 833Combined sources
Helixi99 – 11315Combined sources
Beta strandi116 – 12712Combined sources
Beta strandi129 – 1368Combined sources
Beta strandi141 – 1466Combined sources
Turni153 – 1575Combined sources
Beta strandi158 – 1625Combined sources
Beta strandi164 – 1663Combined sources
Turni169 – 1713Combined sources
Helixi178 – 19114Combined sources
Beta strandi196 – 1983Combined sources
Beta strandi199 – 2013Combined sources
Helixi208 – 2103Combined sources
Turni218 – 2203Combined sources
Helixi228 – 2314Combined sources
Helixi245 – 25511Combined sources
Turni259 – 2624Combined sources
Beta strandi267 – 2693Combined sources
Helixi277 – 2793Combined sources
Beta strandi290 – 2923Combined sources
Beta strandi300 – 3023Combined sources
Beta strandi311 – 3133Combined sources
Beta strandi319 – 3213Combined sources
Beta strandi329 – 3313Combined sources
Beta strandi339 – 3413Combined sources
Beta strandi348 – 3503Combined sources
Beta strandi357 – 3593Combined sources
Beta strandi366 – 3683Combined sources
Beta strandi375 – 3773Combined sources
Beta strandi384 – 3863Combined sources
Helixi390 – 3934Combined sources
Beta strandi395 – 3973Combined sources
Beta strandi399 – 4013Combined sources
Turni406 – 4083Combined sources
Beta strandi410 – 4123Combined sources
Helixi417 – 4204Combined sources
Beta strandi438 – 4447Combined sources
Turni445 – 4484Combined sources
Beta strandi449 – 46113Combined sources
Beta strandi463 – 4708Combined sources
Helixi474 – 4763Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AKLX-ray2.00A10-479[»]
1JIWX-ray1.74P10-479[»]
1KAPX-ray1.64P1-479[»]
3VI1X-ray2.00A/B10-479[»]
ProteinModelPortaliQ03023.
SMRiQ03023. Positions 10-479.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ03023.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati341 – 35414Hemolysin-type calcium-binding 1CuratedAdd
BLAST
Repeati355 – 36713Hemolysin-type calcium-binding 2CuratedAdd
BLAST
Repeati368 – 38518Hemolysin-type calcium-binding 3CuratedAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase M10B family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105QNJ. Bacteria.
COG2931. LUCA.
HOGENOMiHOG000219547.
InParanoidiQ03023.
KOiK01406.
OMAiWYLINSS.
PhylomeDBiQ03023.

Family and domain databases

Gene3Di2.150.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR018511. Hemolysin-typ_Ca-bd_CS.
IPR024079. MetalloPept_cat_dom.
IPR016294. Pept_M10B.
IPR013858. Peptidase_M10B_C.
IPR006026. Peptidase_Metallo.
IPR011049. Serralysin-like_metalloprot_C.
[Graphical view]
PfamiPF08548. 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.

Q03023-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSNSLALKG RSDAYTQVDN FLHAYARGGD ELVNGHPSYT VDQAAEQILR
60 70 80 90 100
EQASWQKAPG DSVLTLSYSF LTKPNDFFNT PWKYVSDIYS LGKFSAFSAQ
110 120 130 140 150
QQAQAKLSLQ SWSDVTNIHF VDAGQGDQGD LTFGNFSSSV GGAAFAFLPD
160 170 180 190 200
VPDALKGQSW YLINSSYSAN VNPANGNYGR QTLTHEIGHT LGLSHPGDYN
210 220 230 240 250
AGEGDPTYAD ATYAEDTRAY SVMSYWEEQN TGQDFKGAYS SAPLLDDIAA
260 270 280 290 300
IQKLYGANLT TRTGDTVYGF NSNTERDFYS ATSSSSKLVF SVWDAGGNDT
310 320 330 340 350
LDFSGFSQNQ KINLNEKALS DVGGLKGNVS IAAGVTVENA IGGSGSDLLI
360 370 380 390 400
GNDVANVLKG GAGNDILYGG LGADQLWGGA GADTFVYGDI AESSAAAPDT
410 420 430 440 450
LRDFVSGQDK IDLSGLDAFV NGGLVLQYVD AFAGKAGQAI LSYDAASKAG
460 470
SLAIDFSGDA HADFAINLIG QATQADIVV
Length:479
Mass (Da):50,433
Last modified:October 1, 1993 - v1
Checksum:i1865EA8F94232663
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti127 – 1271D → H in strain: IFO 3455.
Natural varianti176 – 1761G → A in strain: IFO 3455.
Natural varianti195 – 1973HPG → T in strain: IFO 3455.
Natural varianti350 – 3501I → Y in strain: IFO 3455.
Natural varianti388 – 3892GD → A in strain: IFO 3455.
Natural varianti391 – 3922AE → SP in strain: IFO 3455.
Natural varianti394 – 3963SAA → PPR in strain: IFO 3455.
Natural varianti435 – 4395KAGQA → NAQG in strain: IFO 3455.
Natural varianti454 – 4541I → V in strain: IFO 3455.
Natural varianti460 – 4601A → R in strain: IFO 3455.
Natural varianti479 – 4791V → L in strain: IFO 3455.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64558 Genomic DNA. Translation: CAA45858.1.
AE004091 Genomic DNA. Translation: AAG04638.1.
PIRiA41463.
S26699.
RefSeqiNP_249940.1. NC_002516.2.
WP_003082542.1. NZ_ASJY01000173.1.

Genome annotation databases

EnsemblBacteriaiAAG04638; AAG04638; PA1249.
GeneIDi881248.
KEGGipae:PA1249.
PATRICi19836822. VBIPseAer58763_1297.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64558 Genomic DNA. Translation: CAA45858.1.
AE004091 Genomic DNA. Translation: AAG04638.1.
PIRiA41463.
S26699.
RefSeqiNP_249940.1. NC_002516.2.
WP_003082542.1. NZ_ASJY01000173.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AKLX-ray2.00A10-479[»]
1JIWX-ray1.74P10-479[»]
1KAPX-ray1.64P1-479[»]
3VI1X-ray2.00A/B10-479[»]
ProteinModelPortaliQ03023.
SMRiQ03023. Positions 10-479.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-204154.
STRINGi208964.PA1249.

Protein family/group databases

MEROPSiM10.056.

Proteomic databases

PaxDbiQ03023.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG04638; AAG04638; PA1249.
GeneIDi881248.
KEGGipae:PA1249.
PATRICi19836822. VBIPseAer58763_1297.

Organism-specific databases

PseudoCAPiPA1249.

Phylogenomic databases

eggNOGiENOG4105QNJ. Bacteria.
COG2931. LUCA.
HOGENOMiHOG000219547.
InParanoidiQ03023.
KOiK01406.
OMAiWYLINSS.
PhylomeDBiQ03023.

Enzyme and pathway databases

BRENDAi3.4.24.40. 5087.

Miscellaneous databases

EvolutionaryTraceiQ03023.

Family and domain databases

Gene3Di2.150.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR018511. Hemolysin-typ_Ca-bd_CS.
IPR024079. MetalloPept_cat_dom.
IPR016294. Pept_M10B.
IPR013858. Peptidase_M10B_C.
IPR006026. Peptidase_Metallo.
IPR011049. Serralysin-like_metalloprot_C.
[Graphical view]
PfamiPF08548. 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 nameiAPRA_PSEAE
AccessioniPrimary (citable) accession number: Q03023
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: September 7, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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.