ID   AMPN_CAUVC              Reviewed;         863 AA.
AC   P37893;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Aminopeptidase N;
DE            EC=3.4.11.2;
DE   AltName: Full=Alpha-aminoacylpeptide hydrolase;
GN   Name=pepN; OrderedLocusNames=CC_2481;
OS   Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=190650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=11259647; DOI=10.1073/pnas.061029298;
RA   Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA   Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA   Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA   Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA   Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA   Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT   "Complete genome sequence of Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 725-863.
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=8421698; DOI=10.1073/pnas.90.2.630;
RA   Wang S.P., Sharma P.L., Schoenlein P.V., Ely B.;
RT   "A histidine protein kinase is involved in polar organelle development in
RT   Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:630-634(1993).
CC   -!- FUNCTION: Aminopeptidase N is involved in the degradation of
CC       intracellular peptides generated by protein breakdown during normal
CC       growth as well as in response to nutrient starvation.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR   EMBL; AE005673; AAK24452.1; -; Genomic_DNA.
DR   EMBL; M91449; AAA23051.1; -; Genomic_DNA.
DR   PIR; H87556; H87556.
DR   PIR; S27532; S27532.
DR   RefSeq; NP_421284.1; NC_002696.2.
DR   RefSeq; WP_010920339.1; NC_002696.2.
DR   AlphaFoldDB; P37893; -.
DR   SMR; P37893; -.
DR   STRING; 190650.CC_2481; -.
DR   MEROPS; M01.005; -.
DR   PRIDE; P37893; -.
DR   EnsemblBacteria; AAK24452; AAK24452; CC_2481.
DR   KEGG; ccr:CC_2481; -.
DR   PATRIC; fig|190650.5.peg.2499; -.
DR   eggNOG; COG0308; Bacteria.
DR   HOGENOM; CLU_007993_2_0_5; -.
DR   OMA; FKRWYSQ; -.
DR   BioCyc; CAULO:CC2481-MON; -.
DR   Proteomes; UP000001816; 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   Gene3D; 1.10.390.10; -; 1.
DR   Gene3D; 1.25.50.10; -; 1.
DR   Gene3D; 2.60.40.1730; -; 1.
DR   Gene3D; 2.60.40.1840; -; 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   PANTHER; PTHR46322; PTHR46322; 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; SSF63737; 1.
DR   TIGRFAMs; TIGR02414; pepN_proteo; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Zinc.
FT   CHAIN           1..863
FT                   /note="Aminopeptidase N"
FT                   /id="PRO_0000095068"
FT   ACT_SITE        300
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         124
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         263..267
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         299
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         303
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         322
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   SITE            383
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   863 AA;  94880 MW;  F04BCE19C6A5F7BD CRC64;
     MRTDTPQAVN LADYRPFPFA IETTRLVFDL HPTRTRVSAE LSVRRTGGKN EPLVLNGERL
     KLVSIAIDGR PLAAGEYGVD AERLTIAEAP DAFVLTTEVE IDPSSNKALM GLYMSGGRFC
     TQCEAEGFRT ITYFPDRPDV LSRYSVRIEA DGKFPHLLSN GNPVASGSLD GGRHFAEWSD
     PFPKPSYLFA LVAGDLDVLA DKFITMSGRE VALRVFVDPG QASRAAYALD SLKRAMKWDE
     EAFGREYDLD LFMIVAVRDF NFGAMENKGL NIFNSSLLLA DPQTATDLDY ERIEAVVAHE
     YFHNWTGNRI TCRDWFQLCL KEGFTVFRDQ GLSADMRGAA VQRIKDVRAL RARQFAEDAG
     PLAHPVRPSS YLKIDNFYTA TIYEKGAEII RMLKAILGAP AFRKGCDLYF QRHDGEATTV
     EAFIACFAEA SGRDLSGFFG WYEQAGTPSV TIETAYDAAA GALTLTLTQS TSPTPGQPDK
     KPLPIPIAIG LLAADGRVLR DTEIVLLDQA QMTVRWDSIP EPPVLSALRG FSAPVNLSTD
     ARPSDRYVLF GSDTDLFNRW EAGQTLARDL ILTRAAGAPD EVGEERYADA LGRALVDDAA
     EPAFKALLLA LPSEPDLALM FEAADPAALH AARDHLRTRI AVHLGDLLRR LHGEMQINGE
     FSSDAAAAGR RALRNACAEA LSADPHAENL ARLLGHFGAA RNMTDMIGGL YPMVAMGGVP
     REKALESFHH AWRTEPLVLD KWFAVQGRDP NPDALERVIA LTQHPDFEPT NPNRLRALVS
     TFANFNPARF HDPSGAGYAF LADEILKVDA FNPMTAARLV EPLGGWRRYK PELGDLMRAQ
     LERIVAHPNL SKNVLELASK ALG