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Database: UniProt
Entry: A0A066UFR1_9GAMM
LinkDB: A0A066UFR1_9GAMM
Original site: A0A066UFR1_9GAMM 
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
//
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