ID   A0A239B030_9BACT        Unreviewed;       848 AA.
AC   A0A239B030;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE            EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN   ORFNames=SAMN06296052_10121 {ECO:0000313|EMBL:SNS00598.1};
OS   Pontibacter ummariensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Pontibacter.
OX   NCBI_TaxID=1610492 {ECO:0000313|EMBL:SNS00598.1, ECO:0000313|Proteomes:UP000198432};
RN   [1] {ECO:0000313|Proteomes:UP000198432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NKM1 {ECO:0000313|Proteomes:UP000198432};
RA   Varghese N., Submissions S.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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; FZOQ01000001; SNS00598.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239B030; -.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000198432; Unassembled WGS sequence.
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; cd09603; M1_APN_like; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 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; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533:SF303; AMINOPEPTIDASE N; 1.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000313|EMBL:SNS00598.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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:UP000198432};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..848
FT                   /note="Aminopeptidase N"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012330957"
FT   DOMAIN          72..259
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          297..502
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
SQ   SEQUENCE   848 AA;  96301 MW;  EAEB88200539893E CRC64;
     MNHRFLSIVG LAAAMAFTSA CSANKAVVDT QAAQDVKRKV AVAPADTVPA WAPKKHQFNP
     SRTNVHDLLH TTLRVGFDWE KQYLNGLAEL RLKPYFYPQD SLVLDAKGMD IHSVNLMKGF
     DATPLQYAYD GQKLRIKLDK TYTRNEEYVV EIDYTAKPNE LPAGGSDAIT ADKGLYFINP
     LGEEPNKPQQ IWTQGETEAS SAWFPTIDAP NERMTQDIYI TVDPKFTTLS NGVFMYSRKN
     ADGTKTDYWR QELPHAPYLA MMAIGEFAQV KDKWRDRELT YYVEPEYQGT AKKIFGNTPE
     MMEFFSKKLG VAYPWPKYAQ VVVRDYVSGA MENTSASVFM EDLQLNEREL LDKNWDGIIA
     HELFHQWFGD YVTTESWANL PLNEAFANYS EYLWAEHKFG ADEAAYLQLD ELGQYLDEAE
     TKREPLIRYY YGDKEDMFDA HSYAKGGRVL HMLRKLVGDE AFFASLNRYL TDNKFSAVEV
     AELRMAFEDV TGMDLMWFFD QWFMQPGHPE LQVAQTYQNG QLSLQVKQVQ DTAYMPVYRL
     PLEVAVWAGG KKTTYPIVVD KANQTFTFNT ATKPELVLFD AEQQLLGTVA HEKSEQELLY
     QFYHAGQLAP KLEALTKLEE KLQNPEVLKM YQAALKDDYW RVRSTGINAL SNLSQEQAGV
     VAPTIKQMAL EDEKGAVRAD AVLALAGWGG EKYKAVFEQA MQDSSYQAAA AGIMAYAGTG
     AADIRERLRQ FEEEKNEEIV LALATNYAVQ AGPEKYDWFV RQINQAKGGG LYYLLQSFGA
     FLAGNSETNT PEAINLLAGI AQNHRMYYVR ASAYQALMVM SERPEVQALL NEIRQNETDK
     RLLEMYGQ
//