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Database: UniProt
Entry: A0A1X7E856_9ACTN
LinkDB: A0A1X7E856_9ACTN
Original site: A0A1X7E856_9ACTN 
ID   A0A1X7E856_9ACTN        Unreviewed;       583 AA.
AC   A0A1X7E856;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Membrane-bound lytic murein transglycosylase B {ECO:0000313|EMBL:SMF29325.1};
GN   ORFNames=SAMN02745830_02680 {ECO:0000313|EMBL:SMF29325.1};
OS   Streptomyces sp. Amel2xC10.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1305826 {ECO:0000313|EMBL:SMF29325.1, ECO:0000313|Proteomes:UP000192930};
RN   [1] {ECO:0000313|EMBL:SMF29325.1, ECO:0000313|Proteomes:UP000192930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Amel2xC10 {ECO:0000313|EMBL:SMF29325.1,
RC   ECO:0000313|Proteomes:UP000192930};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FWZW01000005; SMF29325.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7E856; -.
DR   OrthoDB; 9796191at2; -.
DR   Proteomes; UP000192930; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000192930};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..583
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039608251"
FT   DOMAIN          179..231
FT                   /note="Transglycosylase SLT"
FT                   /evidence="ECO:0000259|Pfam:PF13406"
FT   REGION          32..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          266..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          549..583
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..93
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..289
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..324
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        555..583
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   583 AA;  59581 MW;  C1DF7D9D438BB4B6 CRC64;
     MSSAYFGSRL RKGAVNTTVA ALAVAALAAS QAPDVTADSA GRQTTTDAPA ADPATGDGAT
     GNSPYYTDLP PLNSPNPAPS ASTGTTPTGT GSAEAGIPAT VLDAYKKAEA KLAQSKPGCN
     LPWQLLAAIG KVESGQARGG RVSADGTTFA PILGPVLNGV GFANISDTDN GAYDGDSTYD
     RAVGPMQFIP STWEWAGRDG NDDGRKDPNN IYDAALAAGH YLCRYNWDMA TSSGLRSAIL
     SYNNSTDYYN TVISWLEYYR KGSHEIPDGT GSVPSNRSDD DNGTTPRTPA TPAAPHKPGT
     PATPDKPGTP GKPSTPPVTP KPPATPTDTV HHLEDAGTAT LTAMAGDAFT ARIGTRAEAA
     AGKAVAKVRV RFTITGDTDA AFAGGESVAT VVTDSKGVAS APALRAGEKT GAFTVRATVV
     GRTVTALTYR ATVTERAADT LTRAATTDLT CEAGGEFAEE IELKATYGGA AADKVAATAT
     LITSADEPTT NDKGPYFKDA DGNPVRTWTL STDDDGLLKL PKLYADDTAG TYLLRVTTAG
     GATLTLDLTV TAPEPTTPTP DPGESQDPST PPSTTPSPEP GAS
//
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