ID A0A1G1Z4P7_9BACT Unreviewed; 838 AA.
AC A0A1G1Z4P7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=A3E61_01705 {ECO:0000313|EMBL:OGY58890.1};
OS Candidatus Colwellbacteria bacterium RIFCSPHIGHO2_12_FULL_43_12.
OC Bacteria; Candidatus Colwellbacteria.
OX NCBI_TaxID=1797688 {ECO:0000313|EMBL:OGY58890.1, ECO:0000313|Proteomes:UP000178259};
RN [1] {ECO:0000313|EMBL:OGY58890.1, ECO:0000313|Proteomes:UP000178259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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:OGY58890.1}.
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DR EMBL; MHIW01000014; OGY58890.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1Z4P7; -.
DR Proteomes; UP000178259; 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:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 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; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF11838; ERAP1_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:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU364040};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 2..177
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 212..429
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 505..816
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 285
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 370
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 838 AA; 96110 MW; 584AD8F8480447D1 CRC64;
MSIHPNLEEA SFKGEESVTF RLDRAVNKIV LHADELVVSS ASVKIKNKSF ATKRISYDKK
SETVIFLFGQ NLPKGKGKLT LSFTGILNDK MTGFYRSRYK VNGEEHLMAT TQFEATHARQ
AFPCIDEPAA KAVFDITLII PKEHTAISNT IPSVVSEHES GHQIVEFEST PKMSTYLAAF
IVGKFEWIEK KTSKGTLVRV FVTPGKKKQA EFALDVGAKV LAFYEDYFGI KYPLPVLDMI
AIPDFSSGAM ENWGAVTYRE TALLFDTDKS STATKQRVAL VIAHELAHQW FGNLVTMEWW
THLWLNEGFA SYIEYLALDK IFPKWDIWTQ FVYSDLSQAM SLDSLKNTHA IEVEVHHPSE
IGEIFDAVSY SKGASVIRMI ADYLGEKDFR DGLRHYLKKH QYGNASTKDL WLALEHVSDK
PVRSIMDNWT SKPGFPVVII ENDRQKIRLT QSRFFSSSIA KKSSKDKTIW KVPINIKRES
KNRNQEFLLD KKSKSIDLSL KAGEWIYFNS GSSGMYRLNY PEVMLRNLEE AVKRKSIPAR
DRFSIQDDAF ALSESGEFFT VPCLELARSY KNEDDYTVWA SLISNLETVK DLTSGASYPT
LYSAYMRDIL SVIATKVGWE AKRNESHTTP MLRSLVLSVL GYSGDRQTIK RARELFEALK
KGKSLNPDLK GVVYGLVARN GGVKEYEWFL RRHEEESLQE EKNRLLFVLA CFENKKLIKR
ALEYSFSERV RPQDTYGVFS YAWGNRFGRD IVWEFTKSHW DEILKRYGKG GHMLPRFIQP
AGFFASNKKA EEVRRFFRVH KAPGAERAVE QAIEKIYSNA AWLKRDKRKI INWLRSNS
//
