ID A0A1A8TNF7_9GAMM Unreviewed; 877 AA.
AC A0A1A8TNF7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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:SBS34490.1};
GN ORFNames=MSP8886_03082 {ECO:0000313|EMBL:SBS34490.1};
OS Marinomonas spartinae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=1792290 {ECO:0000313|EMBL:SBS34490.1, ECO:0000313|Proteomes:UP000092544};
RN [1] {ECO:0000313|EMBL:SBS34490.1, ECO:0000313|Proteomes:UP000092544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8886 {ECO:0000313|EMBL:SBS34490.1,
RC ECO:0000313|Proteomes:UP000092544};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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; FLOB01000008; SBS34490.1; -; Genomic_DNA.
DR RefSeq; WP_067017986.1; NZ_FLOB01000008.1.
DR AlphaFoldDB; A0A1A8TNF7; -.
DR STRING; 1792290.MSP8886_03082; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000092544; 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; 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:SBS34490.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SBS34490.1};
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:UP000092544};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 110..193
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 232..446
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 451..553
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 557..877
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 877 AA; 98869 MW; EA3B6F3D8B4702E7 CRC64;
MKESQPSAIL LKDYKVPPFL IDKTELTFDL DETNTVVTSH LHMRRNPACG KSTQPLVLDG
GEDIKLIGVA MDGYTLPSEE YRLVDDKLII TATADEFVLT CETLIDPQNN TRLEGLYRSS
SMFCTQCEAE GFRHITYYLD RPDVMSVFTT TIIADETRYP VMLSNGNETE RGKTDEGKTF
VVWHDPFPKP AYLFALVAGD LAVKNDVFTT QSKRDIKLQI FTERHNIDKV NYAMEALKRS
MRWDEETYGR EYDLDIFMIV AVDDFNMGAM ENKGLNIFNS SCLLASPETT TDDAFLRVES
VVAHEYFHNW SGNRVTCRDW FQLSLKEGFT VFRDQSFSSD MHSETVKRVE DVSFLKTAQF
AEDAGPMAHP VRPSSYIEIS NFYTLTVYEK GAEIVRMIHT LLGEEAFRKG SDLYFERHDG
QAVTCDDFVA AMQDASGVDL TLFKRWYSQA GTPVVTVTDE YDEQTKTYRL TVKQHTPATP
AQPTKLSLHI PIRVGLISEQ GDALTADFHN ERSDDFVLHL KDNEQTFEFT SVHSKPIPSL
LRSFSAPVKL HYEYTTEQLL LLLSCDSDGF NRWSAAQQLA VNELSQLIQQ AENGDAFSID
SNLVAGFKAL LEDETLDPAM VALILKLPSQ AYLSELAEVI DPQAIKGARH FLKVTIANAL
AAQFADVYKK HVVMGKYQAN AQDIAHRSLK NTALSYWAES ADQRAQTAVA EQFKQADNMT
DQFAALSIAV KTNHKSAQNM LTAFYEQWKA EPLVVNKWLM LSASQESDDA LGAVKALMEH
PSFDLKNPNK VRSVLGGFGQ NTSGFHHKDG SGYQFLADQI IVLNKRNPQL ASRLCTPLTR
WKKLKPELSV QMKQQLERIL AEDLSKDVYE VVSKSLA
//
