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Database: UniProt
Entry: A0A0S1YA29_9BORD
LinkDB: A0A0S1YA29_9BORD
Original site: A0A0S1YA29_9BORD 
ID   A0A0S1YA29_9BORD        Unreviewed;       473 AA.
AC   A0A0S1YA29;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Type III effector {ECO:0000313|EMBL:ALM86891.1};
GN   ORFNames=ASB57_10560 {ECO:0000313|EMBL:ALM86891.1};
OS   Bordetella sp. N.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1746199 {ECO:0000313|EMBL:ALM86891.1, ECO:0000313|Proteomes:UP000064621};
RN   [1] {ECO:0000313|EMBL:ALM86891.1, ECO:0000313|Proteomes:UP000064621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N {ECO:0000313|EMBL:ALM86891.1,
RC   ECO:0000313|Proteomes:UP000064621};
RA   Hou L.;
RT   "Draft genome of Bordetella sp. N.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP013111; ALM86891.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S1YA29; -.
DR   STRING; 1746199.ASB57_10560; -.
DR   Proteomes; UP000064621; Chromosome.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 1.10.8.350; Bacterial muramidase; 1.
DR   Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR043426; MltB-like.
DR   InterPro; IPR011970; MltB_2.
DR   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
DR   InterPro; IPR031304; SLT_2.
DR   NCBIfam; TIGR02283; MltB_2; 1.
DR   PANTHER; PTHR30163; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE B; 1.
DR   PANTHER; PTHR30163:SF8; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE B; 1.
DR   Pfam; PF01471; PG_binding_1; 1.
DR   Pfam; PF13406; SLT_2; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   SUPFAM; SSF47090; PGBD-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000064621};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..473
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006593382"
FT   DOMAIN          89..392
FT                   /note="Transglycosylase SLT"
FT                   /evidence="ECO:0000259|Pfam:PF13406"
FT   DOMAIN          415..470
FT                   /note="Peptidoglycan binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF01471"
FT   REGION          16..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   473 AA;  50246 MW;  A5949DD28D0F5025 CRC64;
     MLAGLSAALA VSSLPAQAQS GWSSGTPGGD QPTPAKVDPV QAAPAQAAPA QVAPARPATT
     QPAPAQPAIA QPAPALAPAQ AEQDRDPAAC LAKLRVDAPA NGISVADFDR YTQGTKLLAV
     TVAAAKAQPE SKEYWWDYIA KTVDDQRVAE GQAVLQKFGS QLNAIDQNYQ IDSEPLVAIF
     GIETNFGTQF GKVDVLNAWL TRACTEFKPL WVKNVYASTR LLRDGVVQRN DFIGSWSGAF
     GMTQFIPTSF YELAADGDGD GRIDLYHSLP DALASTANHL LKRKAKWTRG LPAVIEVKLP
     GAIAATLPQS PDAEILNSQD RRSLAQWSTA GVTLADGKAL SNVRSGQPWS GVPAYLFAPT
     GARGPVFLAT NNFDAILHYN QARKYALAVS LLTNRLKGDG PLVTPWPTDD PGLSRAQIKQ
     LQQLLATRGY DVGTPDGIPG AKTREAVTTE QGRLGLPQDG RPGGRIFKAL QQQ
//
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