ID A0A3R9R445_9BACT Unreviewed; 895 AA.
AC A0A3R9R445;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=EDE15_3027 {ECO:0000313|EMBL:RSL17492.1};
OS Edaphobacter aggregans.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Edaphobacter.
OX NCBI_TaxID=570835 {ECO:0000313|EMBL:RSL17492.1, ECO:0000313|Proteomes:UP000269669};
RN [1] {ECO:0000313|EMBL:RSL17492.1, ECO:0000313|Proteomes:UP000269669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EB153 {ECO:0000313|EMBL:RSL17492.1,
RC ECO:0000313|Proteomes:UP000269669};
RA Deangelis K.;
RT "Sequencing of bacterial isolates from soil warming experiment in Harvard
RT Forest, Massachusetts, USA.";
RL Submitted (DEC-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:RSL17492.1}.
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DR EMBL; RSDW01000001; RSL17492.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R9R445; -.
DR OrthoDB; 9814383at2; -.
DR Proteomes; UP000269669; 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:UP000269669};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..895
FT /note="Aminopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018664319"
FT DOMAIN 33..235
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 269..485
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 559..872
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 342
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 426
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 895 AA; 98141 MW; 5E942230F5828DFC CRC64;
MLKAGLRRTL LALSALALTA ISAHAQRLPG GAVPEHYTLA LTPDLQAATF TGNETIDLFL
GSPSKTITLN AAEIKIASVQ ATYYPHAVSY VTKGGAGKQN EFSGTIPGKP SFALATVTYD
DAKEQATFIF PNELPAGKVT LDISYTGILN DKLRGFYLSK TKARNYAVTQ FEPTDARRAF
PSFDEPAYKA TFDIALTVDA ADTVISNTNQ IADTPATPGK HTLKFATTPK MSTYLVAFLV
GDFKCTTGKS DGVPIRACST PDKVDMTKFA VESAEYILHY YNTYFGIKYP MPKLDMVALP
DFEAGAMENF GCITYRETDL LVDAKTASIP VKKNVAEVVA HEMAHQWFGD MVTMQWWDNL
WLNEGFATWM ETKPVAKWHP EWNIAQDDAQ ELDNTLNYDS QATTRTIRAK AETPGEINEM
FDGIAYGKAG AVLGMVENYL GEETFRQGVH NYLQAHLYAN ATAEDFWTAQ TSNSHLPVDK
IMESFVTQPG VPLLTFSDAS ASGAPVAQSR FFLSAPANAS TTQQWTLPVC LKTTGKPICR
VLNAGDSTLP IPADAPMTFF YANANSKGYY RTAYTPQQFN AIVAKAETAL TPPERIGLLG
DRWVLVRSGQ GNVGDYLNLV LALKQDPNAA VLENAFGKVN TIDARIATDD DRTQLATVLH
REFSPIYIAL GQPSKSDSFD RQQLRALLFE TLGAAKDPAI VNEARQIADR AFANPGGKDK
TLDPLLTDAA IAIASRNGDV AFYEKVLAAS KDSSDPGQQS EALRTLAHFT DPALVTRTLD
YAVSGQVRNQ DSWIVLAILL NNRETREQTW TYIQQNWDKV HSQFTTNSGV RVVAATGSFC
NINQRDEVKN FFATHKVDAS ERTLSKAIDS INDCIHLRAT QEPSLHQWLA TQSKQ
//
