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Database: UniProt
Entry: A0A0Q6YYB8_9BRAD
LinkDB: A0A0Q6YYB8_9BRAD
Original site: A0A0Q6YYB8_9BRAD 
ID   A0A0Q6YYB8_9BRAD        Unreviewed;       417 AA.
AC   A0A0Q6YYB8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Lytic transglycosylase {ECO:0000313|EMBL:KQW20844.1};
GN   ORFNames=ASC80_11730 {ECO:0000313|EMBL:KQW20844.1};
OS   Afipia sp. Root123D2.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Afipia.
OX   NCBI_TaxID=1736436 {ECO:0000313|EMBL:KQW20844.1, ECO:0000313|Proteomes:UP000051348};
RN   [1] {ECO:0000313|EMBL:KQW20844.1, ECO:0000313|Proteomes:UP000051348}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root123D2 {ECO:0000313|EMBL:KQW20844.1,
RC   ECO:0000313|Proteomes:UP000051348};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQW20844.1, ECO:0000313|Proteomes:UP000051348}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root123D2 {ECO:0000313|EMBL:KQW20844.1,
RC   ECO:0000313|Proteomes:UP000051348};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQW20844.1}.
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DR   EMBL; LMDP01000002; KQW20844.1; -; Genomic_DNA.
DR   RefSeq; WP_056297058.1; NZ_LMDP01000002.1.
DR   AlphaFoldDB; A0A0Q6YYB8; -.
DR   STRING; 1736436.ASC80_11730; -.
DR   OrthoDB; 9808544at2; -.
DR   Proteomes; UP000051348; Unassembled WGS sequence.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 1.10.8.350; Bacterial muramidase; 1.
DR   Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR043426; MltB-like.
DR   InterPro; IPR011970; MltB_2.
DR   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
DR   InterPro; IPR031304; SLT_2.
DR   NCBIfam; TIGR02283; MltB_2; 1.
DR   PANTHER; PTHR30163; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE B; 1.
DR   PANTHER; PTHR30163:SF8; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE B; 1.
DR   Pfam; PF01471; PG_binding_1; 1.
DR   Pfam; PF13406; SLT_2; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   SUPFAM; SSF47090; PGBD-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051348};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..417
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006299482"
FT   DOMAIN          36..338
FT                   /note="Transglycosylase SLT"
FT                   /evidence="ECO:0000259|Pfam:PF13406"
FT   DOMAIN          358..413
FT                   /note="Peptidoglycan binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF01471"
SQ   SEQUENCE   417 AA;  45857 MW;  27B9D58A23BBD7E6 CRC64;
     MRHHGQSRGT SLARSLACAA VLLSALAAPA SADDGFTRFI ASLWPEAQKA GVSRSTFETA
     TRGLQPDYKL PDLVLPGSQP SAAPSQAEFV QVPADYMKEA SIARLAAHGQ GLMRQHRATL
     AAIEQRYGVP STVILAIWAR ETDYGRYALP YNAVRVLATQ AYVGRRKDQF RTEFILALKI
     LEEGHVKLKD MRASWAGAMG LTQFLPSEFY KHAVDFDADG HRNIWTSVPD ALASAAQQLT
     NKGWQPGLRW AYEVKAPRNA DCTEGVPEVT KPIGEWLREG FVPVRGRQLS AAEKAQRASL
     LQPEGIYGPA FLATKNYFVI KEYNYSDLYV LFVGHLSDRM TDPKPFATKW SASSQLRTAD
     VEVMQEHLAK IGLYKDKLDG KAGMLTRAAL GAYQKKAGLK VDCWPSGEVL RAMGAGR
//
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