ID A0A1Q5BI78_9ACTN Unreviewed; 448 AA.
AC A0A1Q5BI78;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Murein transglycosylase {ECO:0000313|EMBL:OKI71029.1};
GN ORFNames=A6A27_20645 {ECO:0000313|EMBL:OKI71029.1};
OS Micromonospora sp. CB01531.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1718947 {ECO:0000313|EMBL:OKI71029.1, ECO:0000313|Proteomes:UP000186700};
RN [1] {ECO:0000313|EMBL:OKI71029.1, ECO:0000313|Proteomes:UP000186700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01531 {ECO:0000313|EMBL:OKI71029.1,
RC ECO:0000313|Proteomes:UP000186700};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKI71029.1}.
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DR EMBL; LWLS01000059; OKI71029.1; -; Genomic_DNA.
DR RefSeq; WP_073834411.1; NZ_LWLS01000059.1.
DR AlphaFoldDB; A0A1Q5BI78; -.
DR STRING; 1718947.A6A27_20645; -.
DR OrthoDB; 9796191at2; -.
DR Proteomes; UP000186700; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd13399; Slt35-like; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR043426; MltB-like.
DR InterPro; IPR031304; SLT_2.
DR PANTHER; PTHR30163; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE B; 1.
DR PANTHER; PTHR30163:SF8; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE B; 1.
DR Pfam; PF13406; SLT_2; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000186700};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 173..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 365..409
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF13406"
FT REGION 1..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..34
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 448 AA; 45645 MW; 42479368B2F6D439 CRC64;
MVDGEERSKV RPLRPAVPPD GAAGPVPVPR PRPATEPGST GTAAGSTHQP ESPPADAPDT
KPQSTADTAA STKAGPTPAD APDVKPQPTP TGAKPESASA DTTATKAEPT SPDAATKAEP
APADATTAGS PDPKTGGRRR MPFAHAVRMP PRRIAVGAAR ATRDWSRRPS GRTTVLGIFL
LLLVAGTATA GALLVPAAVR KPQPVAVDAT ATAPADGVPQ GGVAPGGAGL PPGLPGATGQ
PTGAPPGVGQ PTGPALTGRP ADALAAWAQR VSRTTGIPVV ALQAYGYAQL VLEQTHRSCQ
LSWTTLAAIG YVESRHGAAN GATLQPDGVA SPNILGDLLD GQGGRSRITD TDRGVLDGNT
VYDRALGPMQ FIPSTWQEVG ADADNDGVKN PHDIDDAALA AGQYLCKGGR NMTIPGDWWN
AILSYNDVRR YAQDVFNKAN EYGRLSGT
//