ID E6V0L2_VARPE Unreviewed; 537 AA.
AC E6V0L2;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Lytic transglycosylase catalytic {ECO:0000313|EMBL:ADU36713.1};
GN OrderedLocusNames=Varpa_2513 {ECO:0000313|EMBL:ADU36713.1};
OS Variovorax paradoxus (strain EPS).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU36713.1, ECO:0000313|Proteomes:UP000008917};
RN [1] {ECO:0000313|Proteomes:UP000008917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPS {ECO:0000313|Proteomes:UP000008917};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Ovchinnikova G., Orwin P., Han J.-I.G., Woyke T.;
RT "Complete sequence of Variovorax paradoxus EPS.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADU36713.1, ECO:0000313|Proteomes:UP000008917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPS {ECO:0000313|EMBL:ADU36713.1,
RC ECO:0000313|Proteomes:UP000008917};
RX PubMed=24158554;
RA Han J.I., Spain J.C., Leadbetter J.R., Ovchinnikova G., Goodwin L.A.,
RA Han C.S., Woyke T., Davenport K.W., Orwin P.M.;
RT "Genome of the Root-Associated Plant Growth-Promoting Bacterium Variovorax
RT paradoxus Strain EPS.";
RL Genome Announc. 1:e00843-e00813(2013).
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000256|ARBA:ARBA00007734}.
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DR EMBL; CP002417; ADU36713.1; -; Genomic_DNA.
DR RefSeq; WP_013540944.1; NC_014931.1.
DR AlphaFoldDB; E6V0L2; -.
DR STRING; 595537.Varpa_2513; -.
DR KEGG; vpe:Varpa_2513; -.
DR eggNOG; COG0741; Bacteria.
DR eggNOG; COG1388; Bacteria.
DR HOGENOM; CLU_009520_1_5_4; -.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000008917; Chromosome.
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; 1.
DR CDD; cd16894; MltD-like; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR InterPro; IPR018392; LysM_dom.
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; 2.
DR Pfam; PF01464; SLT; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51782; LYSM; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..537
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003210474"
FT DOMAIN 426..470
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 21..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 537 AA; 58377 MW; 0F3BA28C1334EDFF CRC64;
MKFIAATCLA GSLVLAGCAA PTDNNSSSST SPKIGTTAGG TGSKVAGSAA PVYPRDALSP
LSSGEAHSQS VVTLAPPTDM WDRIRRGFKM PNLESDLVRD REQWYASRPD YIQRMTERSN
KYMFHIVEEL ERRNMPTELA LLPYIESAFN PQAVSSARAA GMWQFMPATG TDFDLKQNIF
RDDRRDVLAS TRAALDYLQK LYGMFGDWQL ALAAYNWGEG SVSRAIAKNQ RAGLPTTYSD
LNMPAETRLY VPKLQAVKNI VANPQAFNAE LPLIANHPYF QTVTLTRDLD VELAAKLADV
RIEDFRALNP AAHKPVLIAA GTPQILLPWD NAAVFQRNFD AYSQGQYASW TAWVVPNTMT
VADAAQRSGM SESDLRAMNN VPPRMLIKAG STLIVPRGAR VKEDVAAVVA DGGHLSFQPE
IVNRRTTVKA GRNDSVASIA RRYKLAPSNV AEWNDVKPNH AFKRGYSVVV YLPVRAAPAA
RVGAGVAVAR GHAAASSKRS SAPAQANTAR GKNVVKVPAG KQVVREKRGG TPSKKKR
//
