ID B0RQE3_XANCB Unreviewed; 560 AA.
AC B0RQE3;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Aminopeptidase {ECO:0000313|EMBL:CAP50678.1};
DE EC=3.4.11.- {ECO:0000313|EMBL:CAP50678.1};
GN ORFNames=XCCB100_1328 {ECO:0000313|EMBL:CAP50678.1};
OS Xanthomonas campestris pv. campestris (strain B100).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=509169 {ECO:0000313|EMBL:CAP50678.1, ECO:0000313|Proteomes:UP000001188};
RN [1] {ECO:0000313|EMBL:CAP50678.1, ECO:0000313|Proteomes:UP000001188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B100 {ECO:0000313|EMBL:CAP50678.1,
RC ECO:0000313|Proteomes:UP000001188};
RX PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA Vorholter F.J., Schneiker S., Goesmann A., Krause L., Bekel T., Kaiser O.,
RA Linke B., Patschkowski T., Ruckert C., Schmid J., Sidhu V.K., Sieber V.,
RA Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K., Puhler A.;
RT "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT the reconstruction of metabolic pathways involved in xanthan
RT biosynthesis.";
RL J. Biotechnol. 134:33-45(2008).
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DR EMBL; AM920689; CAP50678.1; -; Genomic_DNA.
DR AlphaFoldDB; B0RQE3; -.
DR KEGG; xca:xcc-b100_1328; -.
DR HOGENOM; CLU_015077_0_0_6; -.
DR Proteomes; UP000001188; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd09604; M1_APN_like; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF303; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 4: Predicted;
KW Aminopeptidase {ECO:0000313|EMBL:CAP50678.1};
KW Hydrolase {ECO:0000313|EMBL:CAP50678.1};
KW Protease {ECO:0000313|EMBL:CAP50678.1}.
FT DOMAIN 303..459
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 560 AA; 63018 MW; DEB6212474DCEC1C CRC64;
MLWLQLDQNR YRADARAAAS RPSRRSQTTE GMQIASVEVD SGGRRQAVPF LVDDTRLRVD
LPQPLAGQGK ALTVHIRYRY RIPGTWGGRT AVSNSKQGEI YEIAQWYPRM AVYDDLRGWD
TQPYLGSEFY LEYGSFDYAV TVPDGFLVAG SGALTNPDEV LSRTEQQRLA QARGSDRTVL
IRTPAEVAAR AAAPASTRTR TWRFHMDTTR DVAFAASPAF VWDAARINLP DGKQSLAMSV
YPVEGVGEAK WNRSTEYVKG AIEHFSQWYP YPWPAAINLG GYGAGMEYPG IVFDGFDDGG
KDLFWITAHE IGHTWFPMIV GSNERRHAFM DEGFNTFIDV YASDAFNKGE YAPKRDSEYA
PKGGNPVDEI LPLLADANAP TLMDTADATS ETYRHPLTYF KGALGLVLLR EQILGPARFD
PAFRKYIASW AFKHPTPSDF FRLMESESGE DLSWWWRGWY FNNWQLDMGI SEAHYVDQDP
AKGVQVTLRS RQRLVMPVTL RADLADGSHL DRRVPVEAWL QQTAPKLTLA TTQKVLRVRL
DPDHALPDAA RADNTLELAR
//