ID A0A0X3TID7_9GAMM Unreviewed; 557 AA.
AC A0A0X3TID7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Lytic transglycosylase {ECO:0000313|EMBL:KUJ72960.1};
GN ORFNames=AVO41_04115 {ECO:0000313|EMBL:KUJ72960.1};
OS Thiomicrospira sp. WB1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Thiomicrospira.
OX NCBI_TaxID=1685380 {ECO:0000313|EMBL:KUJ72960.1, ECO:0000313|Proteomes:UP000053531};
RN [1] {ECO:0000313|EMBL:KUJ72960.1, ECO:0000313|Proteomes:UP000053531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WB1 {ECO:0000313|EMBL:KUJ72960.1,
RC ECO:0000313|Proteomes:UP000053531};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) 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:KUJ72960.1}.
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DR EMBL; LQBN01000001; KUJ72960.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0X3TID7; -.
DR STRING; 1685380.AVO41_04115; -.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000053531; 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; 3.
DR CDD; cd16894; MltD-like; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 3.
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; 3.
DR Pfam; PF01464; SLT; 1.
DR SMART; SM00257; LysM; 3.
DR SUPFAM; SSF54106; LysM domain; 3.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51782; LYSM; 3.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053531};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..557
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007054070"
FT DOMAIN 392..435
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 456..500
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 509..553
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 557 AA; 63495 MW; B7CB54202AAF476A CRC64;
MTRRTTRLTS WLPRSLAGAG LTLTLSFMTG CAQLSTNFAN PTASTSETTV DSTTGKLPVS
AAPLSATYQT LSIETLETLT LQGLYRLQPL TTQTAQTTAL DQFYVFSEPK PIYDNLWDTI
GDHLFLTPAN THNYQDYIQS YLKKKSYLQR VSKRAKPYLY FILQEIQKRQ MPFEMALLPI
VESGFYPYAR SYMSAAGLWQ FMPATGYMYG LKRSWWYDGR HDVYRSTLAA LDYLQSLYKQ
NNYDWLLALA SYNAGYGNVR KATRRLKRAR PDAPATFWNL QPYLPRETRH YVPQLLAISH
IISHKDRYHI PLEPVANKPF ITTVEIQGQI SLQKVAQKTD MPSSLLKNLN PGFLRQATPP
NGHHKLVLPL DVAEHFKVDY EQAPNQYAVN WRRHQIRSGE NLGLIAQRYG TRVGLIKQLN
NMRSDFIRAG KTLLIPVPGS QATSQVASRS DRADTYRHTV RRGESLWSIA RLYDTSINQL
ARWNGLSRNS TLRPGQTLRV QTSSASRKIS YTLKKGESLW VVARKYQVST DDLCKWNGLS
ANDVLQPGTE LQVWINS
//
