ID A0A3M9N7B1_9BACT Unreviewed; 861 AA.
AC A0A3M9N7B1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=EFA69_01400 {ECO:0000313|EMBL:RNI33103.1};
OS Rufibacter immobilis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Rufibacter.
OX NCBI_TaxID=1348778 {ECO:0000313|EMBL:RNI33103.1, ECO:0000313|Proteomes:UP000271010};
RN [1] {ECO:0000313|EMBL:RNI33103.1, ECO:0000313|Proteomes:UP000271010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCC P1 {ECO:0000313|EMBL:RNI33103.1,
RC ECO:0000313|Proteomes:UP000271010};
RA Yang Y.;
RT "Rufibacter latericius sp. nov., isolated from water in Baiyang Lake.";
RL Submitted (NOV-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RNI33103.1}.
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DR EMBL; RJJE01000001; RNI33103.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M9N7B1; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000271010; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; PF13646; HEAT_2; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 22..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 87..275
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 313..518
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 861 AA; 98562 MW; A09730C7F7FB77D1 CRC64;
MCEINSQLES SKLINHYYMN HILLRALFLF LVVTTGWGCA VKKPSAPAAV AEEVTATPEA
VAAEPAPVTS KGPYQPAAER LVDLLHTTLK VRFDWAKQHL LGEATLTLKP YFYPQDSVVL
DAKGFDIHKV TLLKGRQEVP LQYAYDQYRL TLRLGQRYTR KDTLQLFISY TAKPNELKVK
GSEAILSDKG LYFINPLGTE DGVPQQIWTQ GETEANSAWF PTIDKPNERM TQDLFITVEN
RFKTLSNGVL VSSRKLKDGL RIDHWRMSKP HAPYLAMMAI GEYAVVKDKW RNKEISYWVE
PEYVATAKST FGRTPAMLEF FSQKLGMAFP WDKYAQVVVR DFVSGAMENT TASTFMEALH
QDRRELLDKN WDHIIAHELF HQWFGDLVTT ESWANLPLNE SFADYSEYLW AEHQYGPEEA
ALTHQTALLE YLGESRTKQE PLIRYHYEDK EDMFDSHSYA KGGRVLHMLR QEVGEDAFFA
ALNLYLRQNQ YSAVELDKLR LAFEEVTGRD LKPFFQQWFL TPGHPELAVS HQYENGTLTV
LVQQTQDTVR STVYKFPLVI SLLQEGKWQE QTVQVEKVLE TFRFPMAAAP QTVVVDPRQH
LLARIKHSKS IAEWANQFNY SPGYAAKSNA LEQLRDTADT QIEPVLLKAL QDPFWKIRYM
GVEMLVSTNA MQQPQTQRQV QQMAATDENS SVRAIAMYAL STLQGLPQEI IRRGLEDSSY
LVVSASIFAW AKGEHELEAL KPFLSYKNPD VVNALASAFT GSEQEELYSW YLQNARRMKG
ADLYFFIQSF GAFLLKKKID AQERGWQALV QVVEREAMAE IKQAAFQMLS LMSETDERRE
TLQKLTEQDP GLSPMTGVEI K
//
