ID A0A1G2L389_9BACT Unreviewed; 915 AA.
AC A0A1G2L389;
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=A2934_01955 {ECO:0000313|EMBL:OHA06158.1};
OS Candidatus Sungbacteria bacterium RIFCSPLOWO2_01_FULL_47_10.
OC Bacteria; Candidatus Sungbacteria.
OX NCBI_TaxID=1802276 {ECO:0000313|EMBL:OHA06158.1, ECO:0000313|Proteomes:UP000177982};
RN [1] {ECO:0000313|EMBL:OHA06158.1, ECO:0000313|Proteomes:UP000177982}
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:OHA06158.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MHQO01000037; OHA06158.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2L389; -.
DR Proteomes; UP000177982; 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 55..222
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 257..474
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 553..871
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 330
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 415
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 915 AA; 104121 MW; AD457B283CA69757 CRC64;
MRRTKDAKNP YRLSESVSPT AYFVRWIPNQ KIFALSADTR EHLIKKMNEP EAKELFMFCG
AVEINLSLAR ATETVTLHAH DLKITDGYID KDGIRHGARS VKYNKKYQTA TLSFGKKIGA
GACWLYIEYS GTLNDDMCGA YGTTYQDGDV WRYGIATQFE ATDARRVFPC FDEPAKKATV
EFSLDIPHDL TALSNMPVEY ETSTGAVKIV TFKTTPRMST YLMAFTVMKF EYIEATDRYG
VKVRVYTTPG KKEHGRFGLE VALHTLPALA DYYGMKYPLP KLDLVAIPDF AAGAMENWGI
ETFRETALLV DPKNDSVAAR ERIADVVDHE LAHHWFGNLV TMYWWNHIWL NEGFADFVEN
KMVDLQFPAW ERTLRFISES VLAALHAMDK KNSHPIECEV QNPEEIRENF DTTTYSGGGS
VNLMNEQYLT EEGFRKGLRE YLQTYAYGNA TTQNLWDMIE RATGKPIRSV MGTFTRNTGY
PLVTVEEQEN KEATTRRFKL SQERFLFDGS KDKKNQTWTI PIGTTARNAS KPTYSYMFGK
NMMLEVPVRP GDWVKFNPGT TSLYRVLYPP YIRNELRAAV KAGDLGPADR IGLLDDVFAL
AKAGHVPMVE AVETLSAYEK ESSYYVWSMI AGALGDIDHI LHPGVRMPDD AYTHFREYAK
NFFADPARVM TWNKRGDETN ASILLRALAL RCFGGYGDTE TITTARAKID AFLAGEPLDP
DIRQAVYILN AENGGPEALK KLMRVYDSTE DHQEKIRVLR AIGKTQDPDT VRRVLDLAVS
NKVRKQDTVI VFVNTDKNQA ALPIVWNYIK KNWKLLYARY HGDGIRHLGN IVGVAKRFKT
EDMYRDVKRF FADHPLKGAK RTMAETLEEI RLNIAIRKRD KDSIARWFAE RASARGPVSL
TLTTEALMTE LPELR
//
