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Q60106

- XANP_XANS2

UniProt

Q60106 - XANP_XANS2

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Protein

Xanthomonalisin

Gene
N/A
Organism
Xanthomonas sp. (strain T-22)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

Cleavage of casein.

Cofactori

Binds 1 calcium ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei312 – 3121Charge relay system By similarity
Active sitei316 – 3161Charge relay system By similarity
Active sitei544 – 5441Charge relay system By similarity
Metal bindingi585 – 5851Calcium By similarity
Metal bindingi586 – 5861Calcium; via carbonyl oxygen By similarity
Metal bindingi603 – 6031Calcium; via carbonyl oxygen By similarity
Metal bindingi605 – 6051Calcium By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. serine-type endopeptidase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.21.101. 6720.

Protein family/group databases

MEROPSiS53.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Xanthomonalisin (EC:3.4.21.101)
Alternative name(s):
Carboxyl proteinase
XCP
Xanthomonapepsin
Xanthomonas aspartic proteinase
OrganismiXanthomonas sp. (strain T-22)
Taxonomic identifieri136420 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323 Reviewed predictionAdd
BLAST
Propeptidei24 – 237214Removed in mature formPRO_0000027365Add
BLAST
Chaini238 – 635398XanthomonalisinPRO_0000027366Add
BLAST
Propeptidei636 – 827192Removed in mature formPRO_0000027367Add
BLAST

Post-translational modificationi

Autocatalytically processed.

Keywords - PTMi

Zymogen

Structurei

3D structure databases

ProteinModelPortaliQ60106.
SMRiQ60106. Positions 241-625.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini241 – 625385Peptidase S53Add
BLAST
Domaini635 – 72288PKDAdd
BLAST

Sequence similaritiesi

Contains 1 PKD domain.

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.670. 1 hit.
3.40.50.200. 1 hit.
InterProiIPR007280. Peptidase_C_arc/bac.
IPR015366. Peptidase_S53_propep.
IPR000209. Peptidase_S8/S53_dom.
IPR023828. Peptidase_S8_Ser-AS.
IPR022409. PKD/Chitinase_dom.
IPR000601. PKD_dom.
IPR009020. Prot_inh_propept.
[Graphical view]
PfamiPF00801. PKD. 1 hit.
PF04151. PPC. 1 hit.
PF09286. Pro-kuma_activ. 1 hit.
[Graphical view]
SMARTiSM00089. PKD. 1 hit.
SM00944. Pro-kuma_activ. 1 hit.
[Graphical view]
SUPFAMiSSF49299. SSF49299. 1 hit.
SSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEiPS50093. PKD. 1 hit.
PS51695. SEDOLISIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q60106-1 [UniParc]FASTAAdd to Basket

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MKIEKTALTV AIALAMSSLS AHAEDAWVST HTQAAMSPPA STQVLAASST    50
SATTTGNAYT LNMTGSPRID GAAVTALEAD HPLHVEVALK LRNPDALQTF 100
LAGVTTPGSA LFGKFLTPSQ FTERFGPTQS QVDAVVAHLQ QAGFTNIEVA 150
PNRLLISADG TAGAATNGFR TSIKRFSANG REFFANDAPA LVPASLGDSV 200
NAVLGLQNVS VKHTLHHVYH PEDVTVPGPN VGTQAAAAVA AHHPQDFAAI 250
YGGSSLPAAT NTAVGIITWG SITQTVTDLN SFTSGAGLAT VNSTITKVGS 300
GTFANDPDSN GEWSLDSQDI VGIAGGVKQL IFYTSANGDS SSSGITDAGI 350
TASYNRAVTD NIAKLINVSL GEDETAAQQS GTQAADDAIF QQAVAQGQTF 400
SIASGDAGVY QWSTDPTSGS PGYVANSAGT VKIDLTHYSV SEPASSPYVI 450
QVGGTTLSTS GTTWSGETVW NEGLSAIAPS QGDNNQRLWA TGGGVSLYEA 500
APSWQSSVSS STKRVGPDLA FDAASSSGAL IVVNGSTEQV GGTSLASPLF 550
VGAFARIESA ANNAIGFPAS KFYQAFPTQT SLLHDVTSGN NGYQSHGYTA 600
ATGFDEATGF GSFDIGKLNT YAQANWVTGG GGGSTNAPPV ANFSVATTGL 650
VATFTDSSTD SDGSIASHAW TFGDGSTSTA TSPSHTYSAA GTYSVAETVT 700
DNAGATSTKT SSVTVSSSGG TGGGTVLQNG VAATGLSAAK NGQLKYTVAI 750
PSGAKSLKIA ISGGTGDADL YVKFGSAPTT SSYDCRPYVT GNTESCSFAS 800
PQTGTYYVLL NGYAAFSGVS LKATWTN 827
Length:827
Mass (Da):83,707
Last modified:November 1, 1996 - v1
Checksum:i21A33C4C683DBC8F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D83740 Genomic DNA. Translation: BAA12093.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D83740 Genomic DNA. Translation: BAA12093.1 .

3D structure databases

ProteinModelPortali Q60106.
SMRi Q60106. Positions 241-625.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S53.002.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BRENDAi 3.4.21.101. 6720.

Family and domain databases

Gene3Di 2.60.40.670. 1 hit.
3.40.50.200. 1 hit.
InterProi IPR007280. Peptidase_C_arc/bac.
IPR015366. Peptidase_S53_propep.
IPR000209. Peptidase_S8/S53_dom.
IPR023828. Peptidase_S8_Ser-AS.
IPR022409. PKD/Chitinase_dom.
IPR000601. PKD_dom.
IPR009020. Prot_inh_propept.
[Graphical view ]
Pfami PF00801. PKD. 1 hit.
PF04151. PPC. 1 hit.
PF09286. Pro-kuma_activ. 1 hit.
[Graphical view ]
SMARTi SM00089. PKD. 1 hit.
SM00944. Pro-kuma_activ. 1 hit.
[Graphical view ]
SUPFAMi SSF49299. SSF49299. 1 hit.
SSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEi PS50093. PKD. 1 hit.
PS51695. SEDOLISIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning and expression of an isovaleryl pepstatin-insensitive carboxyl proteinase gene from Xanthomonas sp. T-22."
    Oda K., Ito M., Uchida K., Shibano Y., Fukuhara K., Takahashi S.
    J. Biochem. 120:564-572(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
  2. "Identification of catalytic residues of pepstatin-insensitive carboxyl proteinases from prokaryotes by site-directed mutagenesis."
    Oyama H., Abe S., Ushiyama S., Takahashi S., Oda K.
    J. Biol. Chem. 274:27815-27822(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASPARTIC ACID AND GLUTAMIC ACID RESIDUES, ACTIVE SITES.

Entry informationi

Entry nameiXANP_XANS2
AccessioniPrimary (citable) accession number: Q60106
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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