APEB_PSE14
ID APEB_PSE14 Reviewed; 429 AA.
AC Q48L80;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=PSPPH_1599;
OS Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=264730;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1448A / Race 6;
RX PubMed=16159782; DOI=10.1128/jb.187.18.6488-6498.2005;
RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M.,
RA Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J.,
RA Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., Halpin R.,
RA Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M.,
RA Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A.,
RA Buell R.;
RT "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT 1448A reveals divergence among pathovars in genes involved in virulence and
RT transposition.";
RL J. Bacteriol. 187:6488-6498(2005).
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; CP000058; AAZ33598.1; -; Genomic_DNA.
DR RefSeq; WP_002552650.1; NC_005773.3.
DR AlphaFoldDB; Q48L80; -.
DR SMR; Q48L80; -.
DR STRING; 264730.PSPPH_1599; -.
DR EnsemblBacteria; AAZ33598; AAZ33598; PSPPH_1599.
DR GeneID; 61682461; -.
DR KEGG; psp:PSPPH_1599; -.
DR eggNOG; COG1362; Bacteria.
DR HOGENOM; CLU_019532_2_0_6; -.
DR OMA; GPILKVN; -.
DR OrthoDB; 304020at2; -.
DR Proteomes; UP000000551; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; ISS:JCVI.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; ISS:JCVI.
DR GO; GO:0006508; P:proteolysis; ISS:JCVI.
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; Zinc.
FT CHAIN 1..429
FT /note="Probable M18 family aminopeptidase 2"
FT /id="PRO_1000013700"
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; 46812 MW; EC2B66119DF42478 CRC64;
MRAELNNGLI DFLKASPTPF HATATLVQHF EAAGFQRLDE RDTWAIETGG RYFVTRNDSS
IVAFRMGRQS PLTGGIRMVG AHTDSPCLRV KPQPELQRQG FWQLGVEVYG GALLAPWFDR
DLSLAGRVTF RRDGKVESQL IDFKLPIAVI PNLAIHLNRT ANEGWAINAQ NELPPILAQV
AGDERADFRA LLTDQLAREH GLNADVVLDY ELSFYDTQSA AVVGLNGDFL AGARLDNLLS
CYAGMQALLN SESDETALLV CTDHEEVGSS STCGADGAML EQIVQRLLPS SEDYVRTIQK
SLLISADNAH GIHPNYAEKH DANHGPKLNA GPVIKVNSNQ RYATNSETAG FFRHLCMAEE
VPVQSFVVRS DMACGSTIGP ITASHLGIRT VDIGLPTFAM HSIRELAGSH DLAHLVKVLS
AFYASHELP