ID A0A3M8STK5_9GAMM Unreviewed; 895 AA.
AC A0A3M8STK5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=EER27_13690 {ECO:0000313|EMBL:RNF82554.1};
OS Lysobacter psychrotolerans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1327343 {ECO:0000313|EMBL:RNF82554.1, ECO:0000313|Proteomes:UP000267049};
RN [1] {ECO:0000313|EMBL:RNF82554.1, ECO:0000313|Proteomes:UP000267049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZS60 {ECO:0000313|EMBL:RNF82554.1,
RC ECO:0000313|Proteomes:UP000267049};
RA Luo Y., Sheng H.;
RT "Lysobacter cryohumiis sp. nov., isolated from soil in the Tianshan
RT Mountains, Xinjiang, China.";
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|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:RNF82554.1}.
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DR EMBL; RIBS01000007; RNF82554.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M8STK5; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000267049; 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 Reference proteome {ECO:0000313|Proteomes:UP000267049};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..895
FT /note="Aminopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018169512"
FT DOMAIN 43..226
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 260..477
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 554..860
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 335
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 419
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 895 AA; 97310 MW; 277C3FACE6F71543 CRC64;
MHRYLVSAIA LALASASFTV AAQPPSVSTA VQTTTQLPRN VRPVHYALEV VPHASSLTFD
GKVAITLDVL EPTATITLNA VDIAFASARL AGAGVEASGI VPRILVDTQE QTATFIFDAP
LATGRYVLAM DYRGKIGTQA NGLFAIDYEN RAGKQRALYT QFENSDARKF VPSWDEPNHK
ATFDLTATVP SAQMAVSNMP VTQTTELGDG TKRVRFAQSP RMSTYLLFFG LGDFERATLQ
AGDTEVGVIA QTGSVAQAQF ALESSRDVLR EYNDYFGVPY PLPKLDNIGS PGRSQFFGAM
ENWGAIYTFE YVLLLDPTIA TQADRENVFS VAAHEIAHQW FGDLVTMSWW DDLWLNEGFA
SWLAGRTTEK LHPEWNTAVA AVDVRERAMR RDAVVTTHPV VQHVETVDQA SQAFDSITYS
KGEAVIRMLE GYVGAEAWRD GVRRYIKANA YGNTVSDDLW REVEAAAGKP VTAIAHDFTL
QPGVPMIRVE SARCEGDTTT LVLKQGEFTK DRPDKVPLRW RVPVIAQAIG SDSPVRAVIS
EGEGTMSLPG CAPVLVNAGQ SGYYRTLYAP EQRAAIRDRF TQLRAVDQLG LMGDTWSLGL
VELQPASDYL DLVRATPVDA DPQIWGSVAG RLGELDDFYR DDATQQAAFR AFAIGQLAPV
LARIGWDARP GEAGPVANLR NTLITALGAL GDADVIAQAR RRHAAADRDP AALPAALRTT
VLGVVAQHAD AATWEQLHAQ AKVEKTPLVK DNLYALLSST RDVALARRAL ALSLTDEPGA
TNSAAMIRTV SNQHPDLAFD FAVAHREQVD GMIDSASTSR FYPILATNSL DPAMVGKVRA
YAQAHIVESS RRVSETAVAN ILYRVGVRER VLPVVSAWLS RRGSAARGDI AERAR
//
