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Database: UniProt
Entry: A0A0S4J8L1_BODSA
LinkDB: A0A0S4J8L1_BODSA
Original site: A0A0S4J8L1_BODSA 
ID   A0A0S4J8L1_BODSA        Unreviewed;      1631 AA.
AC   A0A0S4J8L1;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Penicillin amidase, putative {ECO:0000313|EMBL:CUG87601.1};
DE   Flags: Fragment;
GN   ORFNames=BSAL_11030 {ECO:0000313|EMBL:CUG87601.1};
OS   Bodo saltans (Flagellated protozoan).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Eubodonida; Bodonidae; Bodo.
OX   NCBI_TaxID=75058 {ECO:0000313|EMBL:CUG87601.1, ECO:0000313|Proteomes:UP000051952};
RN   [1] {ECO:0000313|Proteomes:UP000051952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lake Konstanz {ECO:0000313|Proteomes:UP000051952};
RG   Pathogen Informatics;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S45 family.
CC       {ECO:0000256|ARBA:ARBA00006586}.
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DR   EMBL; CYKH01001551; CUG87601.1; -; Genomic_DNA.
DR   VEuPathDB; TriTrypDB:BSAL_11030; -.
DR   OrthoDB; 5475521at2759; -.
DR   Proteomes; UP000051952; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.10.1400.10; -; 1.
DR   Gene3D; 2.30.120.10; -; 3.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 3.
DR   Gene3D; 1.10.439.10; Penicillin Amidohydrolase, domain 1; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR043147; Penicillin_amidase_A-knob.
DR   InterPro; IPR023343; Penicillin_amidase_dom1.
DR   InterPro; IPR043146; Penicillin_amidase_N_B-knob.
DR   InterPro; IPR002692; S45.
DR   PANTHER; PTHR34218:SF4; ACYL-HOMOSERINE LACTONE ACYLASE QUIP; 1.
DR   PANTHER; PTHR34218; PEPTIDASE S45 PENICILLIN AMIDASE; 1.
DR   Pfam; PF01804; Penicil_amidase; 3.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 3.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051952};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   TRANSMEM        41..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CUG87601.1"
SQ   SEQUENCE   1631 AA;  180615 MW;  220D288AFDC6D3C6 CRC64;
     LSLFVGYRLI KAKELSLYGA CLFPAEQGTG RKLFRIVTTG VLPTIAFLIT LGLTIGSIAL
     FTLSTSVAPL NKDYTSVPGI SGPIILSRDA AGLTHISASS RADALFGQGF AQAQDRLWQL
     EFQRLAGFPA NRDFVGEDAL DFDKQTRSLN FINATTSICT TFTDRQRALA QSFVDGINYY
     LNTVNERPPE FLFMSKRLLF FHEPEPFTVL DVCMAARILQ WQLSFNIDKE IERFKMFWNT
     DRSYDEIEEM YVNMTNISHT IFNAAQLDLT EEDAVAARAR EAEDHAVERV LYNEYMMNLR
     HTMGGGGSAN ARRVDAAQQQ LQQSRKARKM NSLLKWKAQR ASNAWAGRAA VGSTRSSSAT
     CGASDPHLEI NIPSTWYYSH LTYPDSRNAT FDTSGVSMLG IPGCHVGKTT YVAWGITISQ
     TDLEDLFLLV PDPANPDTHY IVNGTSYAFT PRTEVIQVSG ADDVVLQLQD SIYGPVATEA
     LELPDGLKFA VWARTLQPDT TSATRLFNLG DPDIVRNVRE LRDNVFGQFQ SAGMSIPLLD
     SQGNIGYTMT GLHVLRARGH TGKYPTLGNG SFDHRSAILF TELPTIIINA TTESSAILFS
     AANQKTYPDG YRYTLGYDFD VPYRGARIQY LLRQNTDQLS SYEFHRTVQT DIHSNVWEDM
     QAVMAVNAEF LSLVSADSNG NAWWQALTTA WDGRSSKGSG YPSFFFLWIR ELASVPKDVI
     TALDLNGYWN PVYLYXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
     XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXDHAVE
     RVLYNEYMMN LRHTMGGGSA NAQARRAAAA AEPKRQQGHF EWLYDMDFLK WKAQHASNAW
     AGRAAGPSST TKACGASDPH LDINIPSVWY FSHLTYPDSN NVTFDTSGVG MLGIPGCHIA
     KTTYVAWGIT MSLTDLEDLF LLVPDPANLD THYIVNGTSY AFTPRTEVIK VRGGDDVTLQ
     LQDSLYGPVV TEALKLPDGL KFAVWAKPLR EDNTSITGVF NLGDPDIVRN VRDLRDKGFG
     QLQSPGFSIP MQDAEGNVGY TMTGWHNVTF DTSGVGMLGI PGCHIAKTTY VAWGITMSLT
     DLEDLFLLVP DPANLDTHYI VNGTSYAFTP RTEVIKVRGG DDVTLQLQDS LYGPVVTEAL
     KLPDGLKFAV WAKPLREDNT SITGVFNLGD PDIVRNVRDL RDKGFGQLQS PGFSIPMQDA
     EGNVGYTMTG WHVLRARGHT GKYPTLGNGS FDLRAPIPFD QLPTIIMNAS TLSPASYQPF
     MMSAANQKTY PDGYRYTLGY DFVYPYRGGR IQYLLSQNTD QLSSYEFHRT VQTDIHSNVW
     EDMQAVMAVN AEFLSLVSAD SNGNAWWQAL TTAWDGRSSK GSGYPSFFFL WIRELALVPK
     DVITALDLNG YWNPVYLYPR MLLQAPTVTM TTQCGALTSP ARGSCATFAA QSFNRLAAQY
     AGGEASAPRW GSDLNNLAAT HLMMHGSILE SLFERTVNKD GDYSTIDVSD FSSDLSGSIT
     PSEASSMRQL YDWSTPQNIS FVFPGGDSGN PYSDRYQNLL ELFGDDGYVQ VTVEGALPEA
     EATWARQTLT P
//
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