P58474 (PEPB_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative peptidase B
EC=3.4.11.23

Alternative name(s):
Aminopeptidase B

Gene names

Name:	pepB
Ordered Locus Names:	HI_0875

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › Haemophilus influenzae

Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
Protein existence	Uncertain

General annotation (Comments)

Function	Probably plays an important role in intracellular peptide degradation By similarity. 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 By similarity. HAMAP-Rule MF_00504
Subunit structure	Homohexamer By similarity. HAMAP-Rule MF_00504
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00504.
Sequence similarities	Belongs to the peptidase M17 family.
Caution	Could be the product of a pseudogene.
Sequence caution	The sequence L42023 differs from that shown. Reason: Frameshift at position 340. This may be a natural frameshift.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Manganese Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	Complete proteome 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 – 434	434	Putative peptidase B HAMAP-Rule MF_00504		PRO_0000165836
Sites
	Active site	210	1	Potential
	Active site	284	1	Potential
	Metal binding	198	1	Manganese 2 By similarity
	Metal binding	203	1	Manganese 1 By similarity
	Metal binding	203	1	Manganese 2 By similarity
	Metal binding	221	1	Manganese 2 By similarity
	Metal binding	280	1	Manganese 1 By similarity
	Metal binding	282	1	Manganese 1 By similarity
	Metal binding	282	1	Manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P58474 [UniParc]. Last modified December 13, 2001. Version 1. Checksum: A5A592E51EB18B58	FASTA	434	47,285
	10 20 30 40 50 60 MQITLSNTLA NDAWGKNAIL SFDSNKAMIH LKNNGKTDRT LVQQAARKLR GQGIKEVELV 70 80 90 100 110 120 GEKWDLEFCW AFYQGFYTAK QDYAIEFPHL DDEPQDELLA RIECGDFVRG IINEPAQSLT 130 140 150 160 170 180 PVKLVERAAE FILNQADIYN EKSAVSFKII SGEELEQQGY HGIWTVGKGS ANLPAMLQLD 190 200 210 220 230 240 FNPTQDSNAP VLACLVGKGI TFDSGGYSIK PSDGMSTMRT DMGGAALLTG ALGFAIARGL 250 260 270 280 290 300 NQRVKLYLCC AENLVSNNAF KLGDIITYKN GVSAEVLNTD AEGRLVLADG LIEADNQNPG 310 320 330 340 350 360 FIIDCATLTG AAKSAVGNDY HSVLSMDDEL VKNLFQSAQA ENEPFWRLPF EDFHRSQINS 370 380 390 400 410 420 SFADIANIGS VPVGAGASTA TAFLSYFVKN YKQNWLHIDC SATYRKSGSD LWSVGATGIG 430 VQTLANLMLS RSLK

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. No translation available.
3D structure databases
ProteinModelPortal	P58474.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
OMA	WTRDIIN.
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_HAEIN

Accession

Primary (citable) accession number: P58474

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 13, 2001
Last sequence update:	December 13, 2001
Last modified:	May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program