ID A0A1T5DNW0_9SPHI Unreviewed; 730 AA.
AC A0A1T5DNW0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Transglycosylase {ECO:0000313|EMBL:SKB73418.1};
GN ORFNames=SAMN05661099_2486 {ECO:0000313|EMBL:SKB73418.1};
OS Daejeonella lutea.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Daejeonella.
OX NCBI_TaxID=572036 {ECO:0000313|EMBL:SKB73418.1, ECO:0000313|Proteomes:UP000189981};
RN [1] {ECO:0000313|Proteomes:UP000189981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22385 {ECO:0000313|Proteomes:UP000189981};
RA Varghese N., Submissions S.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FUYR01000002; SKB73418.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5DNW0; -.
DR STRING; 572036.SAMN05661099_2486; -.
DR Proteomes; UP000189981; Unassembled WGS sequence.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016763; F:pentosyltransferase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR011812; Pep_trsgly.
DR PANTHER; PTHR30400:SF0; BIOSYNTHETIC PEPTIDOGLYCAN TRANSGLYCOSYLASE; 1.
DR PANTHER; PTHR30400; MONOFUNCTIONAL BIOSYNTHETIC PEPTIDOGLYCAN TRANSGLYCOSYLASE; 1.
DR Pfam; PF00912; Transgly; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000189981};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 452..598
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT REGION 691..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..730
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 730 AA; 82167 MW; 769589EBAA0E4309 CRC64;
MAKTFLRFNT LSLKRSGNPL MQIPHKYIKI ALITLTSLLV IIIIAGGIAY TKREAILRAA
IQKGITKAKR DYDLDVKIGS ANFTGLSTVS FKNITVVPQD RDSLANIQNF KVGVKLFPLL
FGDIKLSEII LNTGQVNLVK RGSVSNYDFI FRKKSVDSTE KKSELNLSKL ANSLINQLLY
KIPDDMDVRG FEIKFRDDTS ALNFYTTSAT IDGGDVKSTI KVNGNESTWH VEGTVDPGDQ
QLDLIMFADN KKVELPFLEK RLGLKLNFDT ASTQMKGISK RGDILEINGS WGVKNLLVNH
VRISANDIVV PDAYLDADMV IGKNFVSIDS TSTIHVKDIS IHPFIKYTLS PSKVYELKVH
TDEMDAQQVV NSFPQGLFES LEGIQVKGKV KYDLDFHLDE KIPDSVIFKS ELKNIGFKVV
KWGKTNLQKI NKTFVYTPYE YGKPMRDIII GPENPDYVPI DQISPNLKNA LLTAEDPSFY
SHNGFVEESF RNSIITNFKE KAFKRGGSTI SMQLVKNVYL SRQKTMARKA EEMLIVWIIE
NSNLSSKQRM FEVYLNLIEW GRNVYGIGEA ARYYFGKHPS QLDVGEGIFL ASIVPRPKGG
LYRFEGDGSL RQSLRGYFRL IGGLMARRGL TAPDSSAYGF YSVRLREGLR SGIPMVDSLT
ADSLMVGEPE EELTILEQII GKKRPDTVAI KDVNKSKPIS KDTVAAPAET RKQRREQRRE
QREAKKNEDD
//
