ID A0A0M2WJM6_9BURK Unreviewed; 899 AA.
AC A0A0M2WJM6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN Name=pepN_2 {ECO:0000313|EMBL:KKO63076.1};
GN ORFNames=VM94_02821 {ECO:0000313|EMBL:KKO63076.1};
OS Janthinobacterium sp. KBS0711.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=1649647 {ECO:0000313|EMBL:KKO63076.1, ECO:0000313|Proteomes:UP000034315};
RN [1] {ECO:0000313|EMBL:KKO63076.1, ECO:0000313|Proteomes:UP000034315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBS0711 {ECO:0000313|EMBL:KKO63076.1,
RC ECO:0000313|Proteomes:UP000034315};
RA Shoemaker W.R., Muscarella M.E., Lennon J.T.;
RT "Genome sequence of the soil bacterium Jantinobacterium sp. KBS0711.";
RL Submitted (APR-2015) 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:KKO63076.1}.
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DR EMBL; LBCO01000024; KKO63076.1; -; Genomic_DNA.
DR RefSeq; WP_046684019.1; NZ_VCCE02000001.1.
DR AlphaFoldDB; A0A0M2WJM6; -.
DR PATRIC; fig|1649647.5.peg.2891; -.
DR Proteomes; UP000034315; 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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 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:UP000034315};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..899
FT /note="Aminopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005645919"
FT DOMAIN 59..241
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 275..492
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 569..866
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 350
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-2"
FT BINDING 313..317
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-2"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 833
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-2"
FT SITE 434
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 899 AA; 97016 MW; B1A4A7B926B40439 CRC64;
MHRTPTPRFR RSQLAAAVLA LASITAAHAG HAAPAAAPKY ASASHAIGTT TQLPRGVTPL
HYILSITPDA AAPTFKGTAA IKVAVDKPTA SITFNALNLT FAAAAIEGPG GSKQVTRKID
FDADKQTATV HFAQPLAKGE YLLRIDYSGK IGTQATGLFS LDYDTPQGRQ RALYTQFENS
DARSMLPSWD EPDYKATFAL DVVVPSSQMA VGNMPIVRSE ELGNGMKHVY FATTPRMSTY
LLFFGLGDFE RATAMSEGTE IGVITKRGAL AQSRFALDES AALLREYNDY FGVRYPLPKL
DNIAAPGRSQ FFGAMENWGA VFTFEYGLLL DPAISTQADK ENIYTTLSHE MAHQWFGDLV
TMRWWDDLWL NEGFASWMEG RTTERLHPEW NTALSSVGGR ESAMSQDALR TTHPVVQRIA
TVEQASQAFD GITYQKGEAV IRMLEAYVGA DTWRTAVRNY MRKHAYGNTV SDDLWREVDA
AAGKPVSAIA HDFTLQPGVP MIKVGDAVCR NGNTRVRLTQ TEFSKDQPNK KPLSWKVPVI
AATVGNGKLA TVLVKNGKAT LNVPGCGALL VNAGQSGYYR TMYAPANTRA LAGSFARLAP
IDQLGLLADS QSLGLAGAQN LADFLELVQA TPLSADPQVL GKVAGSLGSL YQQYAGDAVR
QQAFGRFAVA RLAPMMAQTG WEARAGEASS VATLRGQLIA ILGDMGEPGV IAEARRRYAA
SEQDPAAMPA PLRRTILGVV AQHADATTWE QLHAKARQEQ TPLVKNQLYD LLASSDDPAL
AQRALALALT DEPGVTNSPA MISRVSRTHP ELAFDFALAH LEQVNARIDA SSRSRYFPRL
AAGSAQADMI AKLEAYAQAH LPASARGDAD SSVAGIKYRI KLRAERLPAV DAWLAKQAG
//
