ID F0B9F9_9XANT Unreviewed; 456 AA.
AC F0B9F9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Leucyl aminopeptidase {ECO:0000313|EMBL:EGD10920.1};
GN ORFNames=XVE_0712 {ECO:0000313|EMBL:EGD10920.1};
OS Xanthomonas vesicatoria ATCC 35937.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=925775 {ECO:0000313|EMBL:EGD10920.1, ECO:0000313|Proteomes:UP000003299};
RN [1] {ECO:0000313|EMBL:EGD10920.1, ECO:0000313|Proteomes:UP000003299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35937 {ECO:0000313|EMBL:EGD10920.1,
RC ECO:0000313|Proteomes:UP000003299};
RX PubMed=21396108; DOI=10.1186/1471-2164-12-146;
RA Potnis N., Krasileva K., Chow V., Almeida N.F., Patil P.B., Ryan R.P.,
RA Sharlach M., Behlau F., Dow J.M., Momol M.T., White F.F., Preston J.F.,
RA Vinatzer B.A., Koebnik R., Setubal J.C., Norman D.J., Staskawicz B.J.,
RA Jones J.B.;
RT "Comparative genomics reveals diversity among xanthomonads infecting tomato
RT and pepper.";
RL BMC Genomics 12:146-146(2011).
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
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:EGD10920.1}.
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DR EMBL; AEQV01000016; EGD10920.1; -; Genomic_DNA.
DR RefSeq; WP_005989294.1; NZ_CP018725.1.
DR AlphaFoldDB; F0B9F9; -.
DR GeneID; 46981839; -.
DR KEGG; xve:BJD12_10655; -.
DR eggNOG; COG0260; Bacteria.
DR Proteomes; UP000003299; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR048816; Peptidase_M17_N_1.
DR PANTHER; PTHR11963:SF53; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF21337; Peptidase_M17_N_1; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:EGD10920.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 304..311
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 456 AA; 48731 MW; 37492FBC85097A6B CRC64;
MSHLTGFTDP AAAALPLYVL DREGFVRWCA EQPTRVLAWA QAQRFDASPG SVLLLPGEQG
LAGAIVGVGD RADAYAYAHA PMALPPASRW RLANSLSDAE LALLHLGWGL GAYRFARYRK
VPRAPAELAA TPSAATRAVI AACLQVRDWV NTPTEDMGPQ QLEDAARAVA QMHGAQVEAI
VGDALLAQNF PTIHAVGRAS HRAPRLIQLQ WGDAAHPHLV LVGKGVCFDT GGLDLKPADG
MRNMKKDMGG AAHALALAGL VMAQQLPVRL TLLIAAVENA VGPDAFRPGE VITTRAGVTV
EVDNTDAEGR LVLCDALSYA TEQRPDLILD FATLTGAARI ALGPDLPALF ANDDALAQAW
ISAGEQTRDP VWRMPLWRPY LRYLNSHVAD MANAGSRMAG AVTAALYLER FVAPGQQWAH
LDVYAWNDSD RPGRPAGGEA LALRSAFAML QQRYGS
//
