ID   BLML_ARTBC              Reviewed;         595 AA.
AC   D4AXL1;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Beta-lactamase-like protein ARB_00930 {ECO:0000305};
DE            EC=3.5.2.6 {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=ARB_00930;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=21919205; DOI=10.1002/pmic.201100234;
RA   Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA   Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT   "Identification of novel secreted proteases during extracellular
RT   proteolysis by dermatophytes at acidic pH.";
RL   Proteomics 11:4422-4433(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC         Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC         ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10102};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21247460,
CC       ECO:0000269|PubMed:21919205}.
CC   -!- SIMILARITY: Belongs to the beta-lactamase family. {ECO:0000305}.
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DR   EMBL; ABSU01000017; EFE32039.1; -; Genomic_DNA.
DR   RefSeq; XP_003012679.1; XM_003012633.1.
DR   AlphaFoldDB; D4AXL1; -.
DR   SMR; D4AXL1; -.
DR   EnsemblFungi; EFE32039; EFE32039; ARB_00930.
DR   GeneID; 9522757; -.
DR   KEGG; abe:ARB_00930; -.
DR   eggNOG; ENOG502RX9C; Eukaryota.
DR   HOGENOM; CLU_019706_2_0_1; -.
DR   OMA; SWQTVDW; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.710.10; -; 1.
DR   InterPro; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   Pfam; PF00144; Beta-lactamase; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..595
FT                   /note="Beta-lactamase-like protein ARB_00930"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000434480"
FT   ACT_SITE        117
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P00811"
FT   ACT_SITE        235
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00811"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        147
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        195
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        249
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        461
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        473
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   595 AA;  65120 MW;  F61F7978FE0CD50B CRC64;
     MVVCFLWLLL PYAATTLSAS VPGCVPSGAL LPRPTELSQS QNIKDATERL SRSLDDAVSG
     RIKAGWDIAN TSFSVSIVSP NGGDPRTGVL WEYHHLAEKN INGTKHLDGD SQYLIGSVSK
     IFSDLLLLKS DVDLQDPITK YLPQLKNASS PIDWDNISLL SLSEHLSGIP ANTIGALQFY
     FLEPLYRALG FPPLNKTDYP PCGIADLNKG CTPEELLTEL VNSHPVSEPY ERPVYSQLSF
     TLFSLALAND TGKDYAQMLE EQVIRPLNLR NTGVSPGEDK RAVIPNVEQQ GWGADYGYNA
     PGGGLYSSLN DLSTLVTKIL DYSILQNPQA TKKWLQPRSA TSSLNTLVGQ PWEILRTSGM
     TPKYPHMIDI YGKSGGAPGY ISQINVIDQY GVGVVLSTAG PLDSRAAYII NEAVLSAILP
     AVEDEARKQA GMYVGEYTSQ KVDNEDATDY APIKLKTVID NGTGIKLESL SRNDSDILEG
     IRKVWSATLS TVGQLASEMR VYPTGLERLA TNDKSLVEQD WRINFDLIPN FNEQASDLPG
     LGKLEALCTS WQTVDWLYYA GVPMDRIVFI VDKEAGRVVG VEIPFLRSGI IQKLN