ID A0A1L7F1V3_9PSEU Unreviewed; 525 AA.
AC A0A1L7F1V3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 28-JUN-2023, entry version 19.
DE SubName: Full=Transglycosylase SLT domain {ECO:0000313|EMBL:APU18801.1};
GN ORFNames=UA75_03845 {ECO:0000313|EMBL:APU18801.1};
OS Actinoalloteichus sp. GBA129-24.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinoalloteichus.
OX NCBI_TaxID=1612551 {ECO:0000313|EMBL:APU18801.1, ECO:0000313|Proteomes:UP000185506};
RN [1] {ECO:0000313|EMBL:APU18801.1, ECO:0000313|Proteomes:UP000185506}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GBA129-24 {ECO:0000313|EMBL:APU18801.1,
RC ECO:0000313|Proteomes:UP000185506};
RA Ruckert C., Nouioui I., Willmese J., van Wezel G., Klenk H.-P.,
RA Kalinowski J., Zotchev S.B.;
RT "Complete genome sequence of Actinoalloteichus fjordicus DSM 46856
RT (=GBA129-24).";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP016077; APU18801.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L7F1V3; -.
DR STRING; 1612551.UA75_03845; -.
DR KEGG; acti:UA75_03845; -.
DR Proteomes; UP000185506; Chromosome.
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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 42..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 225..274
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF13406"
FT REGION 97..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..423
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..440
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 525 AA; 54607 MW; F36FFC17147D727E CRC64;
MSSVIGSARE EGAVLVTIPA QQAYDDSTRT WWRSQRRSSR KVASAAVLFA VMLLPATLGA
VESSPVFPRQ DSDVAELALS DTDSLINLLR HRDDDGGGYG VGGRLPGGTQ ISPEYSQASS
GPGSRDDDDS SVIGPGANAR GIPGVVLEAY LAAEDTLAET MPGCGIEWSL LAGIGRIESN
HARHGMVDAE GTTLSPIIGL QLNGGPGVAA IRDTDGGRLD GDTVWDRAVG PMQFIPSTWA
GYASDGNGDG VSDPHNVFDA SLAAGRYLCS GGLNLRDPAQ LRTAIFRYNR SDVYVGNVLY
WARAYADGVN PLENVTPPSG GSDGGSNSNP NPPQNGPDAP NQPPAPPNPP EPPNPPRPPS
SPEPPPSSSD EPRPPTTTSP QPPWTPEPPE PTDPTDPTEP TDPPDPTDPP DPTDPPDPTE
PCEPPVTDPE DPESPENPED SAETTEPPAP GDPCVPCDPE EPGESEGTDS AESSTEESTE
PPAECEPTEP TEPPSEPGSD SAPQGSVAGT VSSAFRKTMS RSERG
//
