ID A0A066UFR1_9GAMM Unreviewed; 930 AA.
AC A0A066UFR1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=LysM domain-containing protein {ECO:0000313|EMBL:KDN25925.1};
GN ORFNames=MBO_01985 {ECO:0000313|EMBL:KDN25925.1};
OS Moraxella bovoculi 237.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=743974 {ECO:0000313|EMBL:KDN25925.1, ECO:0000313|Proteomes:UP000035860};
RN [1] {ECO:0000313|EMBL:KDN25925.1, ECO:0000313|Proteomes:UP000035860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=237 {ECO:0000313|EMBL:KDN25925.1,
RC ECO:0000313|Proteomes:UP000035860};
RX PubMed=24970830;
RA Calcutt M.J., Foecking M.F., Martin N.T., Mhlanga-Mutangadura T.,
RA Reilly T.J.;
RT "Draft Genome Sequence of Moraxella bovoculi Strain 237T (ATCC BAA-1259T)
RT Isolated from a Calf with Infectious Bovine Keratoconjunctivitis.";
RL Genome Announc. 2:e00612-14(2014).
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:KDN25925.1}.
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DR EMBL; AOMT01000005; KDN25925.1; -; Genomic_DNA.
DR RefSeq; WP_052585232.1; NZ_AOMT01000005.1.
DR AlphaFoldDB; A0A066UFR1; -.
DR eggNOG; COG0741; Bacteria.
DR eggNOG; COG1388; Bacteria.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000035860; 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; 6.
DR CDD; cd16894; MltD-like; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 6.
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:SF26; LYSM DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01476; LysM; 6.
DR Pfam; PF01464; SLT; 1.
DR SMART; SM00257; LysM; 7.
DR SUPFAM; SSF54106; LysM domain; 6.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51782; LYSM; 6.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000035860}.
FT DOMAIN 548..592
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 624..668
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 696..740
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 756..800
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 834..878
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 883..927
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..521
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 930 AA; 99059 MW; 316250ADD482D88C CRC64;
MSHSLSTNDH PDCTKNQKNS RTVGLMKPLT LAVSAYFLAA CSSTGTSTST PTNNTSRTTV
TPTTQSQSSG YSGVLDEAML DELEDLLQAT DMSMVQGDAL TVQRYGNLWD RVRRGYKMGD
TYNARIEAQK SWFYSRQSYL DRLTARASRY LHHTVTEAER RGIPTELALL PIIESSYDPS
ATSNAAAAGL WQFIPSTGRI YGLNQSSSYD GRRDVIESTR AAYDFLTSLY NQFGSWELAL
AAYNAGPGRV SRAIRANEAA GLPTDYWSLN LPTETMNYVP RFIAVSQIVA SPSSYGVNLP
AIANHSHFRT VPVNYGISLQ EIANITGVPF DELRLLNPAL TNFTVDSAGP NRIVIPDSLN
SGVDDQLSAL TGFGYGGSYS ATAPAQTTQY VLPNKGAAVN STSQQELMQS NTLPTTIAQV
TANNTIVQEP PLTQEERDFI AAQIQATTPE AVQAVNPNDG NIQLDALQTA QSVLQARGQS
KSLSYSAPAT TVAVAPQPQP VASEPVIEPS YTPPPVAAPQ QPRPQTNANT SRPAERKPAE
RKPAARPESY TVRSGDTLTG IAAANNLTVN QLASYNNIST NTYVQRGQKL WLVPGKVKPS
PKPAQTATNT ATKTNNTANN TKTATHRVQA GESLTSIARK HDISVHQLAE LNGLSPTDGL
LIGQQIKVPA AKVTNVAPAA NTAPKPASQR ASAQTGAYTV KPGDTLTGIA NSLGVSNADI
AALNNFQPNA GMIAGQVIKV PVSNATVARK LNNQPIKYTV KSGDSLTSVA SRHGITIKEL
ADANDLNTNS NLLLGTTITI PAAGSAKPAR RQSANTKATP SQATPAGNTI ANTENYTVQS
GEHLTGLATR FGVSVNDLAK TNNLATNAQL RRGQVIKVPK LTTTYKVKSG DNLISLARRY
GISTEELAKM NNLANNASLR IGQTLTVPNK
//