ID A0A1F6XLM7_9BACT Unreviewed; 812 AA.
AC A0A1F6XLM7;
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=A2917_01375 {ECO:0000313|EMBL:OGI95077.1};
OS Candidatus Nomurabacteria bacterium RIFCSPLOWO2_01_FULL_42_17.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1801780 {ECO:0000313|EMBL:OGI95077.1, ECO:0000313|Proteomes:UP000178104};
RN [1] {ECO:0000313|EMBL:OGI95077.1, ECO:0000313|Proteomes:UP000178104}
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:OGI95077.1}.
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DR EMBL; MFVE01000008; OGI95077.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6XLM7; -.
DR STRING; 1801780.A2917_01375; -.
DR Proteomes; UP000178104; 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..178
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 213..430
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 481..794
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 286
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 371
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 812 AA; 92905 MW; 530EC5BA24E912F0 CRC64;
MPIEYDIQLK PDLDNFTFWG MEVITLFILK PTKILTLHSK ELEIETVRIA DVYAKISYDE
KKETATFLFP KNILAGKNKL IIVFKGILND KMRGFYRSRY TTGGKEYHMA TTQFEATDAR
RAFPCFDEPA QKAVFYVSLI VPLGKTAISN TLPVSVAEHE AGYQIVKFSP TPKMSTYLLA
FIVGDFEYIE SKTKNNVQVR VFTTPGKKHQ AEFALDCAVK TLEFYEKYFA IAYPLPVLDM
IAIPDFTSGA MENWGAITYR ESALLVDEEH SSLSNKQWVA LVIAHEIAHQ WFGNLVTMEW
WTHLWLNEGF ASYIEYLAID KLFPHWDIWT QFSNNELGTA LRLDALLHTH PIEIPVHHPD
EIGEIFDEVS YSKGASIIRM LADYLGEKDF RDGLRHYLKK HSYKNTETFH LWESFEKISK
KPVAKMMHNW TSEPGYPVVK AQMIKGKINF SQSRFFASPI SAKKVKGKTK WEIPINFKKN
KVNFGEAGFF RTAYSPELLE KLKIPVEKKL LSARDRLGII RDLFALAEAG TIPTTDALEF
LSAYKKEDNY TVWLEIAMGL GRLEQLLAKT DLKARLDGLV FSLFSPLAKK LGWKKKRNEA
HTDALLRSLA ISRAGRAGRS SDEKIINEAR KKFILMQKGK HVHPDLRGAI YSIIAKWGGK
SEYDLFIKKY KKETLHEEKN RIGNALGDFR DPKLLKLACE FAFSNNVRMQ DTIGILSSVG
GNPLGRDIWL NFIQKNWKTL VSRYGDGGHT LARLVKAISG SAEEKHLKAF KKFFATHDAP
GAQRAIEQVK ERLEGNIAWL KRDHEKINNF LL
//
