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Database: UniProt
Entry: F0B9H5_9XANT
LinkDB: F0B9H5_9XANT
Original site: F0B9H5_9XANT 
ID   F0B9H5_9XANT            Unreviewed;       550 AA.
AC   F0B9H5;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Putative aminopeptidase {ECO:0000313|EMBL:EGD10936.1};
GN   ORFNames=XVE_0728 {ECO:0000313|EMBL:EGD10936.1};
OS   Xanthomonas vesicatoria ATCC 35937.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=925775 {ECO:0000313|EMBL:EGD10936.1, ECO:0000313|Proteomes:UP000003299};
RN   [1] {ECO:0000313|EMBL:EGD10936.1, ECO:0000313|Proteomes:UP000003299}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35937 {ECO:0000313|EMBL:EGD10936.1,
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   -!- 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:EGD10936.1}.
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DR   EMBL; AEQV01000016; EGD10936.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0B9H5; -.
DR   eggNOG; COG2234; Bacteria.
DR   Proteomes; UP000003299; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd05660; M28_like_PA; 1.
DR   CDD; cd04821; PA_M28_1_2; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR046450; PA_dom_sf.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147:SF26; ENDOPLASMIC RETICULUM METALLOPEPTIDASE 1; 1.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF52025; PA domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000313|EMBL:EGD10936.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022438, ECO:0000313|EMBL:EGD10936.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022438, ECO:0000313|EMBL:EGD10936.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..550
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003248131"
FT   DOMAIN          128..212
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          299..515
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   550 AA;  59311 MW;  8C2274BF82DA3C65 CRC64;
     MRILLLSACL FVGGVAQAAN DLPGGGIDAE ALSRHVRLLA SDEFEGRAPA SAGEQRTVDY
     LIEQFKAAGV QPGGEEGGWT QAVPLVRAQV DGPVNATLRV GGKTQTLVNG TDVTLQSLRP
     IDKVALKNAP LVFVGYGISA PERQWDDYKG VDLRGKIAVV LINDADFDTA QAGAFDGKAV
     TYYGRWTYKY EEAARRGAAG VLIVHETAPA AYGWATVQSS GLSPLFDIER SDADARAQHV
     PVRGWMQRTL ATSLFKQAGL DFDQAKQRAQ QRDFAPMALG DATLSVDFKL KRERVVTHNV
     VAKLTGSQHP DETVIFSAHW DAFGIGKADA SGDTVRRGAV DNATGVASVL ELARVFAAGP
     KPQRTLYFIA LTAEEKGLLG ANYYAAHPLA PLDKTVAVLN MEMFSPDGPT RDIASWGRGR
     VSLEGDLEQA AKARDRTYSP DPNLEAGFFY RADHFAFARM GVPAITAGPG LDMRKGGVKA
     GKALRDQYFA DCYHQPCDRW TPQWDATGHA ADTTLVYDVG VALANGRQWP SWQDGSEFKA
     IRAKSDAARK
//
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