P45274 (AMPN_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aminopeptidase N
EC=3.4.11.2

Alternative name(s):
Alpha-aminoacylpeptide hydrolase

Gene names

Name:	pepN
Ordered Locus Names:	HI_1614

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	869 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation By similarity.
Catalytic activity	Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subcellular location	Cell inner membrane; Peripheral membrane protein; Cytoplasmic side By similarity.
Sequence similarities	Belongs to the peptidase M1 family.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Ligand	Metal-binding Zinc
Molecular function	Aminopeptidase Hydrolase Metalloprotease Protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding 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 – 869	869	Aminopeptidase N		PRO_0000095070
Regions
	Region	262 – 266	5	Substrate binding By similarity
Sites
	Active site	299	1	Proton acceptor By similarity
	Metal binding	298	1	Zinc; catalytic By similarity
	Metal binding	302	1	Zinc; catalytic By similarity
	Metal binding	321	1	Zinc; catalytic By similarity
	Binding site	122	1	Substrate By similarity
	Site	382	1	Transition state stabilizer By similarity
Experimental info
	Sequence conflict	58	1	Q → G Ref.2
	Sequence conflict	93	1	I → L Ref.2
	Sequence conflict	121	1	C → T Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P45274 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: A00381DC6FB725D1	FASTA	869	99,786
	10 20 30 40 50 60 MLAKAKYRKD YKQPDFTVTD IYLDFQLDPK HTVVTAITKF QRLNNEATSL CLDGHSFQFS 70 80 90 100 110 120 SIKFNGEPFS DYQQDGESLT LDLKDKSADE FEIEIVTFLV PAENTSLQGL YQSGEGICTQ 130 140 150 160 170 180 CEAEGFRQIT YMLDRPDVLA RYITKITADK TKYPFLLSNG NRIASGELED GRHWVEWNDP 190 200 210 220 230 240 FPKPSYLFAL VAGDFDLLQD KFITKSGREV ALELYVDRGN LNRATWAMES LKKAMKWDED 250 260 270 280 290 300 RFNLEYDLDI YMIVAVDFFN MGAMENKGLN IFNSKFVLAN PQTATDDDYL AIESVIAHEY 310 320 330 340 350 360 FHNWTGNRVT CRDWFQLSLK EGLTVFRDQE FSSDTGSRAV NRINNVKFLR TVQFAEDASP 370 380 390 400 410 420 MSHPIRPEKV IEMNNFYTVT VYEKGAEVIR MLHTLLGEQG FQKGMQLYIA ENDGKAATCE 430 440 450 460 470 480 DFVSAMERAN NLDLNQFRRW YSQSGTPELL ISDAYDEKTH TYRLTVSQST PPTADQMEKV 490 500 510 520 530 540 NLHIPLKVAL YDANGTKQML QHNGELLSDV LNVTEKDQVF EFHGIYGRPI PALLCDFSAP 550 560 570 580 590 600 VKLDYDYKTE QLLGLLKFAD NQFIRWDAAQ MLFAQELRRN VVRFQQGEAL EISPEILTAL 610 620 630 640 650 660 SYVLNHYEKD IELATLILTL PKEMEFAESF KTIDPDGISA ARAFMQAQIA ESLKDDFLRV 670 680 690 700 710 720 YTHIRLNDYQ VTQQDIALRV MRNLCLTYLA YTNLGNNLVQ KHYNNANNMT DTLAALSVAT 730 740 750 760 770 780 KAALLCRDVL LADFEQKWQH DGLVMDKWFA LQATRPDDNV LEIIQLLMDH PSFNFNNPNR 790 800 810 820 830 840 LRSLVGSFAN HNLKAFHNVS GSGYRFLTDV LIRLNESNPQ VAARLIEPLI RFSRFDAQRQ 850 860 TLMKRALERL SVVENLSKDL FEKIEKALQ

References

	« Hide 'large scale' referencesShow 'large scale' 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: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
[2]	"Identification of hifD and hifE in the pilus gene cluster of Haemophilus influenzae type b strain Eagan." McCrea K.W., Watson W.J., Gilsdorf J.R., Marrs C.F. Infect. Immun. 62:4922-4928(1994) [PubMed: 7927773] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-129. Strain: Eagan / Serotype B.
[3]	"The fimbrial gene cluster of Haemophilus influenzae type b." van Ham M.S., van Alphen L., Mooi F.R., van Putten J.P.M. Mol. Microbiol. 13:673-684(1994) [PubMed: 7997179] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28. Strain: AM30 (770235) / Serotype B.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC23262.1. Z33502 Genomic DNA. Translation: CAA83910.1. U58657 Genomic DNA. Translation: AAB70877.1.
PIR	F64132.
RefSeq	NP_439756.1. NC_000907.1.
3D structure databases
ProteinModelPortal	P45274.
SMR	P45274. Positions 4-868.
ModBase	Search...
Protein family/group databases
MEROPS	M01.005.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	950613.
GenomeReviews	Gene locus HI_1614 in contig L42023_GR.
KEGG	hin:HI1614.
NMPDR	fig|71421.1.peg.1530.
PATRIC	20191959. VBIHaeInf48452_1687.
TIGR	HI_1614.
Phylogenomic databases
HOGENOM	HBG289207.
OMA	DIFMIVA.
PhylomeDB	P45274.
ProtClustDB	PRK14015.
Enzyme and pathway databases
BioCyc	HINF71421:HI_1614-MONOMER.
Family and domain databases
InterPro	IPR001930. Peptidase_M1. IPR014782. Peptidase_M1_N. IPR012779. Peptidase_M1_pepN. IPR024601. Peptidase_M1_pepN_C. [Graphical view]
Gene3D	G3DSA:1.25.50.10. G3DSA:1.25.50.10. 1 hit.
KO	K01256.
PANTHER	PTHR11533:SF8. Pept_M1_pepN. 1 hit. PTHR11533. Peptidase_M1. 1 hit.
Pfam	PF11940. DUF3458. 1 hit. PF01433. Peptidase_M1. 1 hit. [Graphical view]
PRINTS	PR00756. ALADIPTASE.
TIGRFAMs	TIGR02414. PepN_proteo. 1 hit.
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMPN_HAEIN

Accession

Primary (citable) accession number: P45274

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	January 25, 2012
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program