ID A0A0R2DGH5_9LACO Unreviewed; 844 AA.
AC A0A0R2DGH5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=FD13_GL000938 {ECO:0000313|EMBL:KRN03183.1};
OS Levilactobacillus senmaizukei DSM 21775 = NBRC 103853.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=1423803 {ECO:0000313|EMBL:KRN03183.1, ECO:0000313|Proteomes:UP000051589};
RN [1] {ECO:0000313|EMBL:KRN03183.1, ECO:0000313|Proteomes:UP000051589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21775 {ECO:0000313|EMBL:KRN03183.1,
RC ECO:0000313|Proteomes:UP000051589};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRN03183.1}.
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DR EMBL; AYZH01000002; KRN03183.1; -; Genomic_DNA.
DR RefSeq; WP_061777029.1; NZ_BCWD01000018.1.
DR AlphaFoldDB; A0A0R2DGH5; -.
DR STRING; 1423803.FD13_GL000938; -.
DR PATRIC; fig|1423803.3.peg.938; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000051589; 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; 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 12..181
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 217..435
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 510..816
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 290
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
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 293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 376
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 844 AA; 93243 MW; 874DEE6EB821E1A9 CRC64;
MAESTHFYEL FQPTHYNVYL DINRQAKLIS GTSTITGDAK QTTIAVHQKF MTISAVTADD
QAVPFTFDDE SEGIHITLPG TGVTTLKIDF TAPLTDSMMG IYPSYYEVDG VKKELIGTQF
ETTAARQAFP CVDEPEAKAT FDLAIKFDEK PGETIISNMP EIRNDNGVHV FDTTVRMSTY
LIALAFGDMQ SKITTTKSGV KVGVFATKAH QANELDFALD IAKRAIEFYE DFYQTPYPLP
HSWQLALPDF SAGAMENWGL VTYREAYLLI DPDNTAFDIK GRVATVITHE LAHQWFGDLV
TMKWWDDLWL NESFANMMEY VAVDALEPDW HIWEAFQTGE APMALQRDAT DGVQSVHVQV
ETPAEIDSVF DSAIVYAKGA RMLVMVRALI GDDALRKGLK AYFTAHRYGN ATGADLWAAL
GAASGMDIGA IMHDWLEQPG YPVVSAAVVD GNLTLTQEQF FIGDGKQVGR QWQVPLESNY
QAVPTLLQDQ SLTVGDYADL RQANGKPFRL NQGNSSHFIV KYDDTLLADI LDHADSLDPI
TKLQLLQDLR LLADGRQVSY AEIVPLLDRF SDSKSAVVNT ALYSVAGNLK KFVTPDSDAE
KALKTFFDKI SAAAVSRLGW TAKAGEANDD ELARPTVLNA ALYAKNADAI QAAHDLFTAN
RDHLVALPAA TRVLVLRNEV QNFGSADLFD RLLNAYRTSA DASYKADLSV ALTSTTDAGL
IARLIEKFED ADTIKPQDLR AWYRGVLAND AGEQAAWDWL RNDWQWLEDT VGGDMEFSTY
ITVTSGVFRT AERLAEFKAF FEPKINTPGL TREIQMDTKV VATRVALIEA EASAVNAAVA
QAIK
//