ID K0JP24_SACES Unreviewed; 504 AA.
AC K0JP24;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=TAP domain containing protein {ECO:0000313|EMBL:CCH28150.1};
GN OrderedLocusNames=BN6_08210 {ECO:0000313|EMBL:CCH28150.1};
OS Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / NBRC
OS 15066 / NRRL 15764).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1179773 {ECO:0000313|EMBL:CCH28150.1, ECO:0000313|Proteomes:UP000006281};
RN [1] {ECO:0000313|EMBL:CCH28150.1, ECO:0000313|Proteomes:UP000006281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764
RC {ECO:0000313|Proteomes:UP000006281};
RX PubMed=22958348; DOI=10.1186/1471-2164-13-465;
RA Strobel T., Al-Dilaimi A., Blom J., Gessner A., Kalinowski J.,
RA Luzhetska M., Puhler A., Szczepanowski R., Bechthold A., Ruckert C.;
RT "Complete genome sequence of Saccharothrix espanaensis DSM 44229T and
RT comparison to the other completely sequenced Pseudonocardiaceae.";
RL BMC Genomics 13:465-465(2012).
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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DR EMBL; HE804045; CCH28150.1; -; Genomic_DNA.
DR RefSeq; WP_015098264.1; NC_019673.1.
DR AlphaFoldDB; K0JP24; -.
DR STRING; 1179773.BN6_08210; -.
DR ESTHER; saces-k0jp24; Tiancimycin-TnmK-Tripeptidase-HIP.
DR KEGG; sesp:BN6_08210; -.
DR PATRIC; fig|1179773.3.peg.826; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_013364_3_2_11; -.
DR OMA; HAVYGVF; -.
DR OrthoDB; 4447445at2; -.
DR BioCyc; SESP1179773:BN6_RS04050-MONOMER; -.
DR Proteomes; UP000006281; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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; TRIPEPTIDYL AMINOPEPTIDASE; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF08386; Abhydrolase_4; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000006281};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..504
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003835517"
FT DOMAIN 103..283
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 408..502
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
SQ SEQUENCE 504 AA; 54273 MW; 89A1AE0A16D2D1AE CRC64;
MTRWRTTLVT MAVTAGMAGG VGSAAAAPVE AESAQRGGLS RFHDQRLDWA KCDTEALDAA
GAQCADVTVP LDYERPRGRT ITVAISRLKA ADPAKRRGIM LSNPGGPGNP GLDQLLLVRP
AMSAEVTAQY DLIGMDPRGI GRSSPVDCGW STGFALRAAG PDRKSFDQNH AAQAGLAEQC
AAKEGDRIRH FTTRNTARDL DLVREVLGER KISYFSWSYG TYLGAVYTQM FPQRTDRFVL
DSAIDPARYG PSLLADTGKV NEAALDRWAE WTARRDGEHH LGTTAKQVRA AVEGLIAGSA
KQPIRIGGHT VDAKLLPVLY FILLDRPDRY GPTAAATRNL LEAAAGRQVA IDPLVEGSLL
ALTSGQAAPD ADGQTAVTCG DVAYPGNPDK YWNDIQRNRA KEPVYAAMVR NVSPCAFWPK
PKEKPTVVTN NRPALIVQAT GDTRTPYEHG VNLRKALTGS RLVTLKDVPA HAIFGLYPNK
CVEDQVNTYL ATGTLPARDV TCQG
//