Q60106 (XANP_XANS2) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Xanthomonalisin EC=3.4.21.101 Alternative name(s): Carboxyl proteinase XCP Xanthomonapepsin Xanthomonas aspartic proteinase
Organism	Xanthomonas sp. (strain T-22)
Taxonomic identifier	136420 [NCBI]
Taxonomic lineage	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas

Protein attributes

Sequence length	827 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Cleavage of casein.
Cofactor	Binds 1 calcium ion per subunit By similarity.
Subcellular location	Secreted.
Post-translational modification	Autocatalytically processed.
Sequence similarities	Belongs to the peptidase S53 family. Contains 1 PKD domain.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Protease Serine protease
PTM	Zymogen
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Propeptide	24 – 237	214	Removed in mature form		PRO_0000027365
	Chain	238 – 635	398	Xanthomonalisin		PRO_0000027366
	Propeptide	636 – 827	192	Removed in mature form		PRO_0000027367
Regions
	Domain	635 – 722	88	PKD
Sites
	Active site	312	1	Charge relay system By similarity
	Active site	316	1	Charge relay system By similarity
	Active site	544	1	Charge relay system By similarity
	Metal binding	585	1	Calcium By similarity
	Metal binding	586	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	603	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	605	1	Calcium By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q60106 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 21A33C4C683DBC8F	FASTA	827	83,707
	10 20 30 40 50 60 MKIEKTALTV AIALAMSSLS AHAEDAWVST HTQAAMSPPA STQVLAASST SATTTGNAYT 70 80 90 100 110 120 LNMTGSPRID GAAVTALEAD HPLHVEVALK LRNPDALQTF LAGVTTPGSA LFGKFLTPSQ 130 140 150 160 170 180 FTERFGPTQS QVDAVVAHLQ QAGFTNIEVA PNRLLISADG TAGAATNGFR TSIKRFSANG 190 200 210 220 230 240 REFFANDAPA LVPASLGDSV NAVLGLQNVS VKHTLHHVYH PEDVTVPGPN VGTQAAAAVA 250 260 270 280 290 300 AHHPQDFAAI YGGSSLPAAT NTAVGIITWG SITQTVTDLN SFTSGAGLAT VNSTITKVGS 310 320 330 340 350 360 GTFANDPDSN GEWSLDSQDI VGIAGGVKQL IFYTSANGDS SSSGITDAGI TASYNRAVTD 370 380 390 400 410 420 NIAKLINVSL GEDETAAQQS GTQAADDAIF QQAVAQGQTF SIASGDAGVY QWSTDPTSGS 430 440 450 460 470 480 PGYVANSAGT VKIDLTHYSV SEPASSPYVI QVGGTTLSTS GTTWSGETVW NEGLSAIAPS 490 500 510 520 530 540 QGDNNQRLWA TGGGVSLYEA APSWQSSVSS STKRVGPDLA FDAASSSGAL IVVNGSTEQV 550 560 570 580 590 600 GGTSLASPLF VGAFARIESA ANNAIGFPAS KFYQAFPTQT SLLHDVTSGN NGYQSHGYTA 610 620 630 640 650 660 ATGFDEATGF GSFDIGKLNT YAQANWVTGG GGGSTNAPPV ANFSVATTGL VATFTDSSTD 670 680 690 700 710 720 SDGSIASHAW TFGDGSTSTA TSPSHTYSAA GTYSVAETVT DNAGATSTKT SSVTVSSSGG 730 740 750 760 770 780 TGGGTVLQNG VAATGLSAAK NGQLKYTVAI PSGAKSLKIA ISGGTGDADL YVKFGSAPTT 790 800 810 820 SSYDCRPYVT GNTESCSFAS PQTGTYYVLL NGYAAFSGVS LKATWTN

References

[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D83740 Genomic DNA. Translation: BAA12093.1.
3D structure databases
ProteinModelPortal	Q60106.
SMR	Q60106. Positions 241-625.
ModBase	Search...
Protein family/group databases
MEROPS	S53.002.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BRENDA	3.4.21.101. 6720.
Family and domain databases
Gene3D	2.60.40.670. 1 hit. 3.40.50.200. 1 hit.
InterPro	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]
Pfam	PF00801. PKD. 1 hit. PF04151. PPC. 1 hit. PF09286. Pro-kuma_activ. 1 hit. [Graphical view]
SMART	SM00089. PKD. 1 hit. SM00944. Pro-kuma_activ. 1 hit. [Graphical view]
SUPFAM	SSF52743. Pept_S8_S53. 1 hit. SSF49299. PKD. 1 hit. SSF54897. Prot_inh_propept. 1 hit.
PROSITE	PS50093. PKD. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XANP_XANS2

Accession

Primary (citable) accession number: Q60106

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program