ID   A0A158G6Q8_9BURK        Unreviewed;       517 AA.
AC   A0A158G6Q8;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Tripeptidyl aminopeptidase {ECO:0000313|EMBL:SAL27573.1};
DE            EC=3.4.14.- {ECO:0000313|EMBL:SAL27573.1};
GN   Name=tap_1 {ECO:0000313|EMBL:SAL27573.1};
GN   ORFNames=AWB65_01616 {ECO:0000313|EMBL:SAL27573.1};
OS   Caballeronia humi.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=326474 {ECO:0000313|EMBL:SAL27573.1, ECO:0000313|Proteomes:UP000054977};
RN   [1] {ECO:0000313|EMBL:SAL27573.1, ECO:0000313|Proteomes:UP000054977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 22934 {ECO:0000313|EMBL:SAL27573.1};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family.
CC       {ECO:0000256|ARBA:ARBA00010088}.
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DR   EMBL; FCNW02000005; SAL27573.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158G6Q8; -.
DR   STRING; 326474.AWB65_01616; -.
DR   OrthoDB; 5519806at2; -.
DR   Proteomes; UP000054977; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR013595; Pept_S33_TAP-like_C.
DR   PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR   PANTHER; PTHR43248:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   Pfam; PF08386; Abhydrolase_4; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000313|EMBL:SAL27573.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SAL27573.1};
KW   Protease {ECO:0000313|EMBL:SAL27573.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..517
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011118334"
FT   DOMAIN          99..277
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   DOMAIN          412..504
FT                   /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08386"
SQ   SEQUENCE   517 AA;  54360 MW;  5E63C43B1F9F3F37 CRC64;
     MTSPAKHCVV VAAVCLALVC LMTACSGGGS NGPPALAASF QTVTCPQPNI AGFPDLDFPP
     TVQCGYLTVP ENRTKPDGRR IRIFVMRAPA ASATPRREPV VYLSGGPGGA GSFEVAFMVQ
     HGLNAERDVI FVDQRGTHRA DPLLPCPGWE QFQFDAVSIP FASDSSTAAD VAAIKACHDQ
     LAATGVDLSA YNSTENAADI ADLRVTLGID SWNVYGVSYG SRLALTILRD HPQGIRSVVL
     DSVSPPTVNI VELWWTAPAS SFKAIFAACA AQPTCAKAYP NLASDFTATV NRLDQTPAIT
     QVKDDSGALV TVNVDGFSFA YTMIMESERS DASGVPKMIN DMARGDPGSV AAAYLAFRGP
     HEFVGLGGTG LALDVFCAES ANLTTEAATL AKAQAALPGF PDRVLKIQPK QGRLFYECPV
     WNVGRADPSV SARIVSDVPV LVLEGSFDAA TAPEWVDVIT PDLKNAQVVP FPFTGHSVLG
     KSTCAPAIMA AFLDNPTQPV DSSCAAQTTL TFTTRSP
//