ID A0A261S3A8_9BORD Unreviewed; 470 AA.
AC A0A261S3A8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Lytic transglycosylase {ECO:0000313|EMBL:OZI31477.1};
GN ORFNames=CAL29_26635 {ECO:0000313|EMBL:OZI31477.1};
OS Bordetella genomosp. 10.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1416804 {ECO:0000313|EMBL:OZI31477.1, ECO:0000313|Proteomes:UP000216020};
RN [1] {ECO:0000313|EMBL:OZI31477.1, ECO:0000313|Proteomes:UP000216020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU16122 {ECO:0000313|EMBL:OZI31477.1,
RC ECO:0000313|Proteomes:UP000216020};
RA Spilker T., LiPuma J.;
RT "Complete and WGS of Bordetella genogroups.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000256|ARBA:ARBA00007734}.
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:OZI31477.1}.
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DR EMBL; NEVM01000005; OZI31477.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261S3A8; -.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000216020; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0008933; F:lytic transglycosylase activity; IEA:InterPro.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
DR CDD; cd00118; LysM; 1.
DR CDD; cd16894; MltD-like; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 2.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR000189; Transglyc_AS.
DR InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR PANTHER; PTHR33734; LYSM DOMAIN-CONTAINING GPI-ANCHORED PROTEIN 2; 1.
DR PANTHER; PTHR33734:SF22; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE D; 1.
DR Pfam; PF01476; LysM; 2.
DR Pfam; PF01464; SLT; 1.
DR SMART; SM00257; LysM; 2.
DR SUPFAM; SSF54106; LysM domain; 2.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51782; LYSM; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..470
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012017530"
FT DOMAIN 329..373
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 420..463
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 470 AA; 52147 MW; 8B4FAFBE08F7E925 CRC64;
MKLLRLIVPL LVALLAGCAG TAPKQNFSDA DSKQPGYPNR YVAAVTSRTV DLTHPPRDVW
DRIRRGFAIP NLNTPLTEQW TEYYASHPEA MQRMAERAGK YLYYVTEEIN ERGLPTELAL
LPFVESAYNP TALSRSQASG LWQFVPATGQ HFNLKQDWWR DERRDPIAST NAALDYLESL
FEMQGDWYLA LASYNWGEGS VQRAMAKNAA AGLPTDYLSL QLPEETRNYV PKLQAIKNII
ADPAKYAVVL PPVSNQPYFA TVQKNQDMDV EVAARLAEMP LDEFKALNPS FNRPLIRGEH
APTLILPADR VAIFNANIDA YKGQLSSWKV YSARRGESYA SIAKRFGVSE STLRQVNEIP
HRQKAAVAQN LLVPGNTGGV QVASLDMSSG AERAEFKPAV AQRQGRLASV KPNAVKPNVR
QHKVRNGDTL FSLARQYGTS VDALRALNNL RGNNLKVGST LRVPGTNVRG
//
