ID Q2KZ48_BORA1 Unreviewed; 898 AA.
AC Q2KZ48;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN Name=pepN {ECO:0000313|EMBL:CAJ49767.1};
GN OrderedLocusNames=BAV2157 {ECO:0000313|EMBL:CAJ49767.1};
OS Bordetella avium (strain 197N).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ49767.1, ECO:0000313|Proteomes:UP000001977};
RN [1] {ECO:0000313|EMBL:CAJ49767.1, ECO:0000313|Proteomes:UP000001977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N {ECO:0000313|EMBL:CAJ49767.1,
RC ECO:0000313|Proteomes:UP000001977};
RX PubMed=16885469; DOI=10.1128/JB.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC amino acids including Pro (slow action). When a terminal hydrophobic
CC residue is followed by a prolyl residue, the two may be released as
CC an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000098};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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DR EMBL; AM167904; CAJ49767.1; -; Genomic_DNA.
DR RefSeq; WP_012417821.1; NC_010645.1.
DR AlphaFoldDB; Q2KZ48; -.
DR STRING; 360910.BAV2157; -.
DR MEROPS; M01.005; -.
DR GeneID; 41393996; -.
DR KEGG; bav:BAV2157; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_007993_2_0_4; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000001977; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09600; M1_APN; 1.
DR Gene3D; 2.60.40.1840; -; 1.
DR Gene3D; 3.30.2010.30; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 1.25.50.10; Peptidase M1, alanyl aminopeptidase, C-terminal domain; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR038438; PepN_Ig-like_sf.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR012779; Peptidase_M1_pepN.
DR InterPro; IPR024601; Peptidase_M1_pepN_C.
DR InterPro; IPR037144; Peptidase_M1_pepN_C_sf.
DR InterPro; IPR035414; Peptidase_M1_pepN_Ig-like.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR NCBIfam; TIGR02414; pepN_proteo; 1.
DR PANTHER; PTHR46322; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR PANTHER; PTHR46322:SF1; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR Pfam; PF11940; DUF3458; 1.
DR Pfam; PF17432; DUF3458_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:CAJ49767.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAJ49767.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001977};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 106..188
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 227..443
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 462..569
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 573..895
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 898 AA; 100131 MW; 52BD3D1F4E35BAE4 CRC64;
MRTDTPVTVY RKDYLPYPYA IPEVALSFDL DPESTLVTSR LRLERKPEAA VDAPLELDGE
ELALQSLRVD GQDWTDYQLD EQRLVIRGLP ALCTLEIGAR CRPSANSSLM GLYVSGGNFF
TQCEAEGFRR ITWFADRPDV MSRYRVTLRA DARYPVLLSN GNLLSTRQLP DGRQEAQWED
PFLKPCYLFA LVAGNLTHRE KQVRTRSGRE VLLQVYSDPG SESRTAWALE SLERALRWDE
TRFGLELDLD RFMVVAVRDF NMGAMENKGL NIFNAAYVLA DPQTATDVNY EGIESVIGHE
YFHNWTGNRV TCRDWFQLSL KEGLTVFRDQ EFSADMMAHG LDPAAAASAR AVKRIDDVAT
LRAAQFPEDA GPMAHPIRPD SYQEIGNFYT ATVYEKGAEV IRMQHTLLGE AGFRAGMDEY
FRRHDGQAVT CDDFVNAMDS VYQQLNPGRD LSVFRNWYRQ AGTPRVAVTL HQDGDRLTVT
LKQHCAPVGV EKQAGVNAVK QPFHIPFAFG LLDRQGRPLS LKLNGVEIGE TALLELRETS
KSWVFEDVPE GVLPSLLRGF SAPVIVEYNW TEAELALLCA HDSDPFARWE AGQELASRQL
LALAASHQAQ QPLTVNQGFI AAWRTQLTDP ALDAAYRARA LALPAEKTLA ERMPAIDPPA
LAVARDFLRA ELGRQLAAEW QAIFEANQEE GPYSPAPGPA GKRALKNLAL AYLMANESAQ
ALRLAQHQYD NADNMTDSMA ALACLVNYAP RPIAQAALDH FYARWQNDPL VVDKWFTLQA
AARSSGLPEI RALMAHPAFT LRNPNRARAL VFQFCLNNAR SMHAADGSGH AFWAEQVLAL
DALNPEIAAR LARAMDNWSR FTPALRGSMQ AALQGVRSHE GLSRNVTEIV SKALEFSA
//
