APEB_PSEPK
ID APEB_PSEPK Reviewed; 429 AA.
AC Q88M44;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Probable M18 family aminopeptidase 2 {ECO:0000255|HAMAP-Rule:MF_00467};
DE EC=3.4.11.- {ECO:0000255|HAMAP-Rule:MF_00467};
GN Name=apeB {ECO:0000255|HAMAP-Rule:MF_00467}; OrderedLocusNames=PP_1730;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00467};
CC -!- SIMILARITY: Belongs to the peptidase M18 family. {ECO:0000255|HAMAP-
CC Rule:MF_00467}.
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DR EMBL; AE015451; AAN67351.1; -; Genomic_DNA.
DR RefSeq; NP_743887.1; NC_002947.4.
DR RefSeq; WP_010952777.1; NC_002947.4.
DR AlphaFoldDB; Q88M44; -.
DR SMR; Q88M44; -.
DR STRING; 160488.PP_1730; -.
DR EnsemblBacteria; AAN67351; AAN67351; PP_1730.
DR KEGG; ppu:PP_1730; -.
DR PATRIC; fig|160488.4.peg.1824; -.
DR eggNOG; COG1362; Bacteria.
DR HOGENOM; CLU_019532_2_0_6; -.
DR OMA; GPILKVN; -.
DR PhylomeDB; Q88M44; -.
DR BioCyc; PPUT160488:G1G01-1831-MON; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.250.10; -; 1.
DR HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR InterPro; IPR022984; M18_aminopeptidase_2.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; PTHR28570; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
PE 3: Inferred from homology;
KW Aminopeptidase; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..429
FT /note="Probable M18 family aminopeptidase 2"
FT /id="PRO_0000173466"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00467"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00467"
FT BINDING 401
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00467"
SQ SEQUENCE 429 AA; 46996 MW; F1EEE02EC45B033D CRC64;
MRDALNTGLI EFLKASPTPF HATASLVQRL EAAGYKRLDE RDSWDTETGG RYYVTRNDSS
IIAIKLGKQS PLLNGIRMVG AHTDSPCLRV KPQPELQRQG FLQLGVEVYG GALLAPWFDR
DLSLAGRVTY RRDGKVESQL IDFKLPVAII PNLAIHLNRT ANEGWAINPQ NELPPILAQV
AGDERIDFRA LLTEQLAREH ELIADVVLDY ELSFYDTQDA ALIGLNGDFI AGARLDNLLS
CYAGLQALLA ADSDETCVLV CNDHEEVGSC SACGADGPML EQTLQRLLPD GDTYVRTVQR
SLMVSADNAH GVHPNYADKH DGNHGPKLNA GPVIKVNNNQ RYATNSETAG FFRHLCMAEE
VPVQSFVVRS DMGCGSTIGP ITASHLGVRT VDIGLPTFAM HSIRELCGSH DLAHLVKVLT
AFYRSRELP