Q9RF52 (PEPB_SALTY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidase B
EC=3.4.11.23

Alternative name(s):
Aminopeptidase B

Gene names

Name:	pepB
Ordered Locus Names:	STM2536

Organism

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]

Taxonomic identifier

99287 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella choleraesuis › Salmonella enterica I › Salmonella typhimurium

Protein attributes

Sequence length	427 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probably plays an important role in intracellular peptide degradation. HAMAP-Rule MF_00504
Catalytic activity	Release of an N-terminal amino acid, Xaa, from a peptide or arylamide. Xaa is preferably Glu or Asp but may be other amino acids, including Leu, Met, His, Cys and Gln. HAMAP-Rule MF_00504
Cofactor	Binds 2 manganese ions per subunit.
Subunit structure	Homohexamer.
Subcellular location	Cytoplasm HAMAP-Rule MF_00504.
Sequence similarities	Belongs to the peptidase M17 family.
Biophysicochemical properties	pH dependence: Optimum pH is 8.5-9.5. HAMAP-Rule MF_00504

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Manganese Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	aminopeptidase activity Inferred from electronic annotation. Source: HAMAP manganese ion binding Inferred from electronic annotation. Source: HAMAP metalloexopeptidase 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
	Chain	1 – 427	427	Peptidase B HAMAP-Rule MF_00504		PRO_0000165842
Sites
	Active site	207	1	Potential
	Active site	281	1	Potential
	Metal binding	195	1	Manganese 2 By similarity
	Metal binding	200	1	Manganese 1 By similarity
	Metal binding	200	1	Manganese 2 By similarity
	Metal binding	218	1	Manganese 2 By similarity
	Metal binding	277	1	Manganese 1 By similarity
	Metal binding	279	1	Manganese 1 By similarity
	Metal binding	279	1	Manganese 2 By similarity
Experimental info
	Mutagenesis	310	1	K → V: Reduces the ability to hydrolyze Asp-Leu without decreasing its ability to hydrolyze Leu-Leu. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9RF52 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 37CCAE4C8771F499	FASTA	427	46,355
	10 20 30 40 50 60 MTEAMKITLS TQPADARWGD KATYSINNDG ITLHLNGKDD LGLIQRAARK IDGLGIKQVA 70 80 90 100 110 120 LTGEGWDTER CWAFWAGYKG PKGVRTVMWP DLDDAQRQEL DNRLTIIDWV RDTINAPAEE 130 140 150 160 170 180 LGPEQLAQRA VDLLCSVACD SVTYRITKGE DLREQNYMGL HTVGRGSERP PVLLALDYNP 190 200 210 220 230 240 TGDKDAPVYA CLVGKGITFD SGGYSIKQSA FMDSMKSDMG GAATVTGALA FAITRGLNKR 250 260 270 280 290 300 VKLFLCCADN LISGNAFKLG DIIRYRNGKN VEVMNTDAEG RLVLADGLID ASAQHPQLII 310 320 330 340 350 360 DMATLTGAAK TALGNDYHAL FSFDDTLAGR LLTSAAQENE PFWRLPLAEF HRNQLPSNFA 370 380 390 400 410 420 ELNNTGSAAY PAGASTAAGF LSHFVENYRE GWLHIDCSAT YRKAPVEQWA AGATGLGVRT IANLLTA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Salmonella enterica serovar typhimurium peptidase B is a leucyl aminopeptidase with specificity for acidic amino acids." Mathew Z., Knox T.M., Miller C.G. J. Bacteriol. 182:3383-3393(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION, MUTAGENESIS OF LYS-310. Strain: LT2 and TN5179.
[2]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF201078 Genomic DNA. Translation: AAF19377.1. AE006468 Genomic DNA. Translation: AAL21430.1.
RefSeq	NP_461471.1. NC_003197.1.
3D structure databases
ProteinModelPortal	Q9RF52.
ModBase	Search...
Protein-protein interaction databases
STRING	99287.STM2536.
Protein family/group databases
MEROPS	M17.004.
Proteomic databases
PaxDb	Q9RF52.
PRIDE	Q9RF52.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAL21430; AAL21430; STM2536.
GeneID	1254058.
KEGG	stm:STM2536.
PATRIC	32383707. VBISalEnt20916_2676.
Phylogenomic databases
eggNOG	COG0260.
HOGENOM	HOG000243130.
KO	K07751.
OMA	ENEAFWR.
ProtClustDB	PRK05015.
Enzyme and pathway databases
BRENDA	3.4.11.1. 2169.
Family and domain databases
HAMAP	MF_00504. Aminopeptidase_M17.
InterPro	IPR011356. Leucine_aapep/pepB. IPR008330. Pept_M17_PepB. IPR000819. Peptidase_M17_C. [Graphical view]
PANTHER	PTHR11963:SF3. PTHR11963:SF3. 1 hit.
Pfam	PF12404. DUF3663. 1 hit. PF00883. Peptidase_M17. 1 hit. [Graphical view]
PIRSF	PIRSF036388. Ctsl_amnpptdse_B. 1 hit.
PRINTS	PR00481. LAMNOPPTDASE.
PROSITE	PS00631. CYTOSOL_AP. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PEPB_SALTY

Accession

Primary (citable) accession number: Q9RF52

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 13, 2001
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program