Q05308 (SP1_RARFA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Serine protease 1 EC=3.4.21.- Alternative name(s): Serine protease I Short name=RPI
Organism	Rarobacter faecitabidus
Taxonomic identifier	13243 [NCBI]
Taxonomic lineage	cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Rarobacteraceae › Rarobacter

Protein attributes

Sequence length	525 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)

Function	Major serine protease exhibiting lytic activity toward living yeast cells. Similar to elastase in its substrate specificity and has a lectin-like affinity for mannose. Mannoproteins may be the native substrate for RPI.
Subcellular location	Secreted.
Sequence similarities	Belongs to the peptidase S1 family. Contains 1 ricin B-type lectin domain.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Lectin Mannose-binding
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Zymogen
Technical term	Direct protein sequencing
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	mannose 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 – 32	32	Potential
	Propeptide	33 – 211	179	Potential		PRO_0000026919
	Chain	212 – 525	314	Serine protease 1		PRO_0000026920
Regions
	Domain	396 – 525	130	Ricin B-type lectin
	Region	401 – 525	125	Essential for the lytic activity, but not for protease function
Sites
	Active site	238	1	Charge relay system By similarity
	Active site	270	1	Charge relay system By similarity
	Active site	352	1	Charge relay system By similarity
Amino acid modifications
	Disulfide bond	223 ↔ 239		By similarity
	Disulfide bond	310 ↔ 320		By similarity
	Disulfide bond	346 ↔ 376		By similarity
	Disulfide bond	412 ↔ 431		By similarity
	Disulfide bond	453 ↔ 472		By similarity
	Disulfide bond	496 ↔ 514		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q05308 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: DA2BCF7D330EBB61	FASTA	525	55,654
	10 20 30 40 50 60 MKCKKPSALF SALALVGALG AASVLGAASA NSASPVAAAT VQASSGSAKT SVAATSKSQD 70 80 90 100 110 120 GDVLAAIVRD LKITKTQAKK RIKLEEKARQ LEPRLQKKLG KKFAGLWISK NGKKIVVGVT 130 140 150 160 170 180 TKKAAKVVKK AGATPKIVKS NLTTLKKRAT KISKNAPSDI KNVNSWWVDP ATNKVVIEAR 190 200 210 220 230 240 SKKAAKAAAT AAGLTAGTYE ITVSDDVIVP VRDYWGGDAL SGCTLAFPVY GGFLTAGHCA 250 260 270 280 290 300 VEGKGHILKT EMTGGQIGTV EASQFGDGID AAWAKNYGDW NGRGRVTHWN GGGGVDIKGS 310 320 330 340 350 360 NEAAVGAHMC KSGRTTKWTC GYLLRKDVSV NYGNGHIVTL NETSACALGG DSGGAYVWND 370 380 390 400 410 420 QAQGITSGSN MDTNNCRSFY QPVNTVLNKW KLSLVTSTDV TTSYVQGYQN NCIDVPNSDF 430 440 450 460 470 480 TDGKQLQVWN CNGTNAQKVS FHPDGTLRIN GKCLDARWAW THNGTEVQLM NCNGHIAQKF 490 500 510 520 TLNGAGDLVN VHANKCVDVK DWGGQGGKLQ LWECSGGANQ KWWRR

References

[1]	"Molecular structure of Rarobacter faecitabidus protease I. A yeast-lytic serine protease having mannose-binding activity." Shimoi H., Iimura Y., Obata T., Tadenuma M. J. Biol. Chem. 267:25189-25195(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 212-222; 224-238 AND 240-244. Strain: YLM-50.
[2]	"Characterization of Rarobacter faecitabidus protease I, a yeast-lytic serine protease having mannose-binding activity." Shimoi H., Tadenuma M. J. Biochem. 110:608-613(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 212-247.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D10753 Genomic DNA. Translation: BAA01585.1.
PIR	A45053.
3D structure databases
ProteinModelPortal	Q05308.
ModBase	Search...
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13.
MEROPS	S01.276.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR004236. Pept_S1_alpha_lytic. IPR001316. Pept_S1A_streptogrisin. IPR000772. Ricin_B_lectin. IPR009003. Trypsin-like_Pept_dom. [Graphical view]
Pfam	PF02983. Pro_Al_protease. 1 hit. PF00652. Ricin_B_lectin. 1 hit. [Graphical view]
PRINTS	PR00861. ALYTICPTASE.
SMART	SM00458. RICIN. 1 hit. [Graphical view]
SUPFAM	SSF50494. Pept_Ser_Cys. 1 hit. SSF50370. RicinB_like. 1 hit.
PROSITE	PS50231. RICIN_B_LECTIN. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SP1_RARFA

Accession

Primary (citable) accession number: Q05308

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	April 3, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program