ID A0A1W6ZHN2_9BORD Unreviewed; 732 AA.
AC A0A1W6ZHN2;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Lytic transglycosylase {ECO:0000313|EMBL:ARP96918.1};
GN ORFNames=CAL15_22645 {ECO:0000313|EMBL:ARP96918.1};
OS Bordetella genomosp. 13.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=463040 {ECO:0000313|EMBL:ARP96918.1, ECO:0000313|Proteomes:UP000194161};
RN [1] {ECO:0000313|EMBL:ARP96918.1, ECO:0000313|Proteomes:UP000194161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU7206 {ECO:0000313|EMBL:ARP96918.1,
RC ECO:0000313|Proteomes:UP000194161};
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}.
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DR EMBL; CP021111; ARP96918.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6ZHN2; -.
DR STRING; 463040.CAL15_22645; -.
DR KEGG; bgm:CAL15_22645; -.
DR OrthoDB; 92254at2; -.
DR Proteomes; UP000194161; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR CDD; cd13401; Slt70-like; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 1.25.20.10; Bacterial muramidases; 1.
DR Gene3D; 1.10.1240.20; Lytic transglycosylase, superhelical linker domain; 1.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR037061; Lytic_TGlycoase_superhlx_L_sf.
DR InterPro; IPR012289; Lytic_TGlycosylase_superhlx_L.
DR InterPro; IPR008939; Lytic_TGlycosylase_superhlx_U.
DR InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR PANTHER; PTHR37423:SF2; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE; 1.
DR PANTHER; PTHR37423; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE-RELATED; 1.
DR Pfam; PF01464; SLT; 1.
DR Pfam; PF14718; SLT_L; 1.
DR SUPFAM; SSF48435; Bacterial muramidases; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 485..544
FT /note="Lytic transglycosylase superhelical linker"
FT /evidence="ECO:0000259|Pfam:PF14718"
FT DOMAIN 565..669
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 732 AA; 80949 MW; 345795ABF16817AC CRC64;
MQRDRQSGPY QKSTMTVRRA PDAAPSCPSS STFRRWLPAL ALVATACSSV DAQQRADAPM
GAANAVATVT PAANAGVLEQ QAQVQAQTPR PISVPRVELA GLPPSPNDAA RQAVVASREA
MNRKQWSALG MAAPQAANDP LGIYAQYWLL RYQLWNPPGG QRPTAALQRF LQANAGTYLE
DKLRSDWIIV AARSGDFETV QDLGEPRVPN SQVACARVDA QHMTGKRATA AQAVAVFQPV
TACWKLYDQL VADRVLGWEH IQPQVRDAVE DNDLADANKL GEYIFEADDR KQLAILLKDP
MKWLVRQSKS PVGRNEKELV TLALARLARS DIAVADSYLR REWESHLPKA DVAWVRTQYA
LIAALNLDER AHRWYREAGE SVRMTPYNHA WRVRAALREP KVDWKWVLAS IAQMSPAQQA
EPAWVYWKSR GLAAQGHGEQ ARQGYASIAD QFNFYGQLAA EELGRKITVP PVPQPVTDAE
MAQARANPGL IRAVHLFRLG WRGEAVPEWN FSLRGMSDRQ LMAAAELARA EGLFDRVVNT
SDRTEAEFDF TQRYIAPFEG RVSAKARAIA LDPAWVYGLI RQESRFVMEA RSHVGASGLM
QLMPATAKWV ARKIGMNDFT PDSVHDFDVN TELGTNYLNM VLQDLGGSQL LASAGYNAGP
RRPINWRATF SHPVEGAIFA ETIPFTETRQ YVQNVMSNAT YYAALFSGQP QSLKARLGSV
GATGPVARTE LP
//
