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Database: UniProt
Entry: A0A0Q5V5L1_9CAUL
LinkDB: A0A0Q5V5L1_9CAUL
Original site: A0A0Q5V5L1_9CAUL 
ID   A0A0Q5V5L1_9CAUL        Unreviewed;       426 AA.
AC   A0A0Q5V5L1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Lytic murein transglycosylase {ECO:0000313|EMBL:KQS55820.1};
GN   ORFNames=ASG17_07105 {ECO:0000313|EMBL:KQS55820.1};
OS   Brevundimonas sp. Leaf363.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=1736353 {ECO:0000313|EMBL:KQS55820.1, ECO:0000313|Proteomes:UP000051182};
RN   [1] {ECO:0000313|EMBL:KQS55820.1, ECO:0000313|Proteomes:UP000051182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf363 {ECO:0000313|EMBL:KQS55820.1,
RC   ECO:0000313|Proteomes:UP000051182};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQS55820.1, ECO:0000313|Proteomes:UP000051182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf363 {ECO:0000313|EMBL:KQS55820.1,
RC   ECO:0000313|Proteomes:UP000051182};
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:KQS55820.1}.
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DR   EMBL; LMPZ01000002; KQS55820.1; -; Genomic_DNA.
DR   RefSeq; WP_056101077.1; NZ_LMPZ01000002.1.
DR   AlphaFoldDB; A0A0Q5V5L1; -.
DR   STRING; 1736353.ASG17_07105; -.
DR   OrthoDB; 9808544at2; -.
DR   Proteomes; UP000051182; 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:UP000051182};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..426
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006265460"
FT   DOMAIN          68..346
FT                   /note="Transglycosylase SLT"
FT                   /evidence="ECO:0000259|Pfam:PF13406"
FT   DOMAIN          367..417
FT                   /note="Peptidoglycan binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF01471"
FT   REGION          26..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..43
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   426 AA;  45330 MW;  737FC1A86CC920A5 CRC64;
     MRASFRLLLI GAVAACAPML PEAPPILPSP PAPQGPAPAP VPAPSNQTAE QTAADAAGFE
     GWKQGFLSRQ GGARRAAYEQ ELAGVTPDAS VIRLDRNQPE FSRPAGAYVQ NAVTAVRIAQ
     AKQRVDRVPW PVVQRYGVPS EILVGVWAQE SAFGQVQGDY DVIRSLATLA YDGRRREWAE
     GQLKNALDIV IDGRRSRAGL KGSWAGAMGQ TQFMPDSYLR LGVDQDGDGK VDIWSTDADA
     LASAANLLAT EGWKRGQTWG YEVILPAGFD YAEAEGPKHP WSYWAQRGVR LAAGGAPTSD
     EAAEGAAILL PQGARGPAFL ALPNHYVIRK YNNSVSYALA IGLTADGIVG KPALTGTWPN
     DAPLSRDQRI GAQSALTRLG FDTGGVDGVV GANTRAALRR WQVANNRLAD GYLTADLADE
     LVRIAN
//
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