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Database: UniProt
Entry: A0A0Q6MKR1_9BURK
LinkDB: A0A0Q6MKR1_9BURK
Original site: A0A0Q6MKR1_9BURK 
ID   A0A0Q6MKR1_9BURK        Unreviewed;       425 AA.
AC   A0A0Q6MKR1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Glycosyl transferase family 51 domain-containing protein {ECO:0000259|Pfam:PF00912};
GN   ORFNames=ASC88_21115 {ECO:0000313|EMBL:KQU78310.1};
OS   Rhizobacter sp. Root29.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX   NCBI_TaxID=1736511 {ECO:0000313|EMBL:KQU78310.1, ECO:0000313|Proteomes:UP000051195};
RN   [1] {ECO:0000313|EMBL:KQU78310.1, ECO:0000313|Proteomes:UP000051195}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root29 {ECO:0000313|EMBL:KQU78310.1,
RC   ECO:0000313|Proteomes:UP000051195};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQU78310.1, ECO:0000313|Proteomes:UP000051195}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root29 {ECO:0000313|EMBL:KQU78310.1,
RC   ECO:0000313|Proteomes:UP000051195};
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:KQU78310.1}.
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DR   EMBL; LMCN01000009; KQU78310.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q6MKR1; -.
DR   STRING; 1736511.ASC88_21115; -.
DR   Proteomes; UP000051195; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; IEA:InterPro.
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};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051195};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          229..383
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   REGION          385..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   425 AA;  46132 MW;  CD0EA2DCEB063AB6 CRC64;
     MWITGVLAAL LLALLVGGWA MLRLLRPVDG EWAQTLHIGP WQRAISMPAV IRLATHPVML
     RVLEGRTVRT PFGRVAIAPD GPDAWRATCA PCALRGIGLP GDAVRLTRLV VTLARDADMN
     LQGDFALGEP AHAVRGRWRA VLTPQRLELN VQGDVTPIAD AFALFASTIP ELPHAQVDGL
     MRFDLRLRLP ERTLEFRPRL DGFRVAGLGT EALLNAAPNC NTDGAVPAGG FGTWLPRAVI
     AAEDQRFHEH TGYDLDEIGH ALSFEPQRGA STLSQQLARL VYTGGARGHA RKLRELLYAV
     ELDRTLGKAR VMHLYLSLVP WGQGRCGAHA AAAQLLHKRV DKLTPAEAAW LASLLHNPDL
     ELARFDARGE VNAARVRWVL SQMRPVPRTP KPPARGGNAT RAVPEDATAA PPAPIQQALA
     LALAR
//
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