ID   A0A257T0A5_9GAMM        Unreviewed;       546 AA.
AC   A0A257T0A5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=LysM domain-containing protein {ECO:0000259|PROSITE:PS51782};
GN   ORFNames=B7Z66_00420 {ECO:0000313|EMBL:OYV78071.1};
OS   Chromatiales bacterium 21-64-14.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales.
OX   NCBI_TaxID=1970504 {ECO:0000313|EMBL:OYV78071.1, ECO:0000313|Proteomes:UP000215939};
RN   [1] {ECO:0000313|EMBL:OYV78071.1, ECO:0000313|Proteomes:UP000215939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=21-64-14 {ECO:0000313|EMBL:OYV78071.1};
RA   Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA   Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT   "Lifting the veil on microbial sulfur biogeochemistry in mining
RT   wastewaters.";
RL   Submitted (MAR-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:OYV78071.1}.
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DR   EMBL; NCBI01000001; OYV78071.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257T0A5; -.
DR   Proteomes; UP000215939; 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;
FT   DOMAIN          346..389
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          420..464
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          491..535
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
SQ   SEQUENCE   546 AA;  60943 MW;  6CF2F89B457A9AFA CRC64;
     MTCARLKECT LFVGLLALLG VSGCSGLRPP IGEGTNAIAP ASATAAAPQA TVAVPTQTAP
     ADQMDQANAE PPNLWSRLRA GFGLPHPDNA RVIAERDWYA RHPKYLDRAF IRSEPFLYFI
     QQQVEVRHMP SEIALLPVVE SAFQPFAYSH GRAAGLWQFI PSTGRRFGLK QNWWYDGRRD
     IYASTRAALD YLEQLKDQFN GDWLLALAAY NSGAGTVQAA IQRNQRLGRP TDFWHLDLPS
     ETQAYVPKLL ALGELVANPK RYDLTLPTVP DKPYFAVVQI RSQIDLARVA ELSGLPLDQV
     YKLNPGFNRW ATDPHGPHRL LLPKADAVTF LRKLAVLPED EHVSWTRHQI RPGETLSQIA
     RHYHTTVALL QQVNHLRGIE IRAGSHLVIP VAQESLAHYR LSADQRRLAL LHTPRVGEKM
     VHTVRPGDTL WNIARSFGVP VHTLARWNGI APGDVLKPGR KLVIWKRGLT TTVAYRAPAG
     PPARLGVVQT IRYTVRRGDS LARISQRFKV SVAQLCHWNE LSARGILHPG QRLTLHVNVM
     RQADSI
//