ID   A0A2G5J0P5_9ACTN        Unreviewed;       517 AA.
AC   A0A2G5J0P5;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Peptidase {ECO:0000313|EMBL:PIB10323.1};
GN   ORFNames=B1C81_07445 {ECO:0000313|EMBL:PIB10323.1};
OS   Streptomyces sp. HG99.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1958787 {ECO:0000313|EMBL:PIB10323.1, ECO:0000313|Proteomes:UP000231274};
RN   [1] {ECO:0000313|EMBL:PIB10323.1, ECO:0000313|Proteomes:UP000231274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HG99 {ECO:0000313|EMBL:PIB10323.1,
RC   ECO:0000313|Proteomes:UP000231274};
RA   Li Y.;
RT   "Diversity and bioprospecting of biosynthetic gene clusters of culturable
RT   actinobacteria from Tibetan Plateau, China.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family.
CC       {ECO:0000256|ARBA:ARBA00010088}.
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:PIB10323.1}.
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DR   EMBL; MVDM01000003; PIB10323.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5J0P5; -.
DR   Proteomes; UP000231274; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000231274};
KW   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_5039598334"
FT   DOMAIN          117..288
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   DOMAIN          411..516
FT                   /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08386"
FT   REGION          22..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   517 AA;  54260 MW;  50FFC29E98B83EA5 CRC64;
     MTRFARWTAA AAAALLVAGC SSGSSGDGTD EGKNSDTPSA AASSSGAAAG LPASLTSQKL
     DWGRCKGTSD SPAPGSGWQC ATLKVPLDYA KPDGETIGLA LIRSKATGGE SKRIGSLLFN
     FGGPGGSGVS TMPAYESVVG PLHQRYDLVS WDPRGVATSE GVRCRSDKAI QAAESVDATP
     DDAAEEAAYF KDAADFGKGC EKAQGKLLSH VSTTDTARDM DLMRHILGDR RMHYFGISYG
     TELGGVYAHL FPQKVGRLIL DAVVDPSADT VGHAKNQTLG FQRALDDYLK STGKDPKQGS
     QKIVDLLDRI DTKPLPTSGG RKLTETLALT GIILPLYSKE SWPTLTSALK AAEDGDGSQL
     LGLADGYNSR DASGHYGTTT HSQRVISCLD DKQRPTPEET ETLLPEFEKI SPVFGDYLGW
     DTAGWCHDWP VGGQFDNPEV SAPGAEPILV VGNTGDPATP YEGARRMADE LGKGVGVQLT
     WKGEGHGAYG SGSDCVDSTV NSYLLDGTVP KDGKVCS
//