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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)DescriptionActionsGraphical viewLength
Metal bindingi185Zinc; via tele nitrogen; catalytic1
Active sitei1861
Metal bindingi189Zinc; via tele nitrogen; catalytic1
Metal bindingi195Zinc; via tele nitrogen; catalytic1
Metal bindingi262Calcium 1; via carbonyl oxygen1
Metal bindingi264Calcium 1; via carbonyl oxygen1
Metal bindingi266Calcium 11
Metal bindingi294Calcium 11
Metal bindingi296Calcium 1; via carbonyl oxygen1
Metal bindingi297Calcium 2; via carbonyl oxygen1
Metal bindingi299Calcium 11
Metal bindingi299Calcium 21
Metal bindingi336Calcium 2; via carbonyl oxygen1
Metal bindingi338Calcium 21
Metal bindingi343Calcium 3; via carbonyl oxygen1
Metal bindingi345Calcium 3; via carbonyl oxygen1
Metal bindingi347Calcium 31
Metal bindingi352Calcium 4; via carbonyl oxygen1
Metal bindingi354Calcium 4; via carbonyl oxygen1
Metal bindingi356Calcium 41
Metal bindingi360Calcium 3; via carbonyl oxygen1
Metal bindingi361Calcium 5; via carbonyl oxygen1
Metal bindingi362Calcium 3; via carbonyl oxygen1
Metal bindingi363Calcium 5; via carbonyl oxygen1
Metal bindingi365Calcium 31
Metal bindingi365Calcium 51
Metal bindingi369Calcium 4; via carbonyl oxygen1
Metal bindingi370Calcium 6; via carbonyl oxygen1
Metal bindingi371Calcium 4; via carbonyl oxygen1
Metal bindingi372Calcium 6; via carbonyl oxygen1
Metal bindingi374Calcium 41
Metal bindingi374Calcium 61
Metal bindingi378Calcium 5; via carbonyl oxygen1
Metal bindingi379Calcium 7; via carbonyl oxygen1
Metal bindingi380Calcium 5; via carbonyl oxygen1
Metal bindingi381Calcium 7; via carbonyl oxygen1
Metal bindingi383Calcium 51
Metal bindingi383Calcium 71
Metal bindingi392Calcium 6; via carbonyl oxygen1
Metal bindingi399Calcium 61
Metal bindingi409Calcium 71
Metal bindingi455Calcium 81
Metal bindingi457Calcium 81
Metal bindingi459Calcium 81
Metal bindingi461Calcium 8; via carbonyl oxygen1
Metal bindingi463Calcium 81

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)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000286811 – 99
ChainiPRO_000002868210 – 479SerralysinAdd BLAST470

Keywords - PTMi

Zymogen

Proteomic databases

PaxDbiQ03023.
PRIDEiQ03023.

Interactioni

Protein-protein interaction databases

MINTiMINT-204154.
STRINGi208964.PA1249.

Structurei

Secondary structure

1479
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 22Combined sources10
Turni23 – 25Combined sources3
Beta strandi29 – 33Combined sources5
Helixi41 – 48Combined sources8
Turni49 – 51Combined sources3
Beta strandi62 – 70Combined sources9
Helixi76 – 79Combined sources4
Helixi81 – 83Combined sources3
Helixi99 – 113Combined sources15
Beta strandi116 – 127Combined sources12
Beta strandi129 – 136Combined sources8
Beta strandi141 – 146Combined sources6
Turni153 – 157Combined sources5
Beta strandi158 – 162Combined sources5
Beta strandi164 – 166Combined sources3
Turni169 – 171Combined sources3
Helixi178 – 191Combined sources14
Beta strandi196 – 198Combined sources3
Beta strandi199 – 201Combined sources3
Helixi208 – 210Combined sources3
Turni218 – 220Combined sources3
Helixi228 – 231Combined sources4
Helixi245 – 255Combined sources11
Turni259 – 262Combined sources4
Beta strandi267 – 269Combined sources3
Helixi277 – 279Combined sources3
Beta strandi290 – 292Combined sources3
Beta strandi300 – 302Combined sources3
Beta strandi311 – 313Combined sources3
Beta strandi319 – 321Combined sources3
Beta strandi329 – 331Combined sources3
Beta strandi339 – 341Combined sources3
Beta strandi348 – 350Combined sources3
Beta strandi357 – 359Combined sources3
Beta strandi366 – 368Combined sources3
Beta strandi375 – 377Combined sources3
Beta strandi384 – 386Combined sources3
Helixi390 – 393Combined sources4
Beta strandi395 – 397Combined sources3
Beta strandi399 – 401Combined sources3
Turni406 – 408Combined sources3
Beta strandi410 – 412Combined sources3
Helixi417 – 420Combined sources4
Beta strandi438 – 444Combined sources7
Turni445 – 448Combined sources4
Beta strandi449 – 461Combined sources13
Beta strandi463 – 470Combined sources8
Helixi474 – 476Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ03023.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati341 – 354Hemolysin-type calcium-binding 1CuratedAdd BLAST14
Repeati355 – 367Hemolysin-type calcium-binding 2CuratedAdd BLAST13
Repeati368 – 385Hemolysin-type calcium-binding 3CuratedAdd BLAST18

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)DescriptionActionsGraphical viewLength
Natural varianti127D → H in strain: IFO 3455. 1
Natural varianti176G → A in strain: IFO 3455. 1
Natural varianti195 – 197HPG → T in strain: IFO 3455. 3
Natural varianti350I → Y in strain: IFO 3455. 1
Natural varianti388 – 389GD → A in strain: IFO 3455. 2
Natural varianti391 – 392AE → SP in strain: IFO 3455. 2
Natural varianti394 – 396SAA → PPR in strain: IFO 3455. 3
Natural varianti435 – 439KAGQA → NAQG in strain: IFO 3455. 5
Natural varianti454I → V in strain: IFO 3455. 1
Natural varianti460A → R in strain: IFO 3455. 1
Natural varianti479V → L in strain: IFO 3455. 1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AKLX-ray2.00A10-479[»]
1JIWX-ray1.74P10-479[»]
1KAPX-ray1.64P1-479[»]
3VI1X-ray2.00A/B10-479[»]
ProteinModelPortaliQ03023.
SMRiQ03023.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-204154.
STRINGi208964.PA1249.

Protein family/group databases

MEROPSiM10.056.

Proteomic databases

PaxDbiQ03023.
PRIDEiQ03023.

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: November 2, 2016
This is version 133 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.