ID A0A0Q5E6T1_9BURK Unreviewed; 1058 AA.
AC A0A0Q5E6T1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=ASF61_00240 {ECO:0000313|EMBL:KQQ47129.1};
OS Duganella sp. Leaf126.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1736266 {ECO:0000313|EMBL:KQQ47129.1, ECO:0000313|Proteomes:UP000051032};
RN [1] {ECO:0000313|EMBL:KQQ47129.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ47129.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ47129.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ47129.1};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.1.129;
CC Evidence={ECO:0000256|ARBA:ARBA00023988};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000256|ARBA:ARBA00007090}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
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:KQQ47129.1}.
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DR EMBL; LMNW01000001; KQQ47129.1; -; Genomic_DNA.
DR RefSeq; WP_056149888.1; NZ_LMNW01000001.1.
DR AlphaFoldDB; A0A0Q5E6T1; -.
DR STRING; 1736266.ASF61_00240; -.
DR OrthoDB; 8552189at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000051032; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; 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 Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 2.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transferase {ECO:0000313|EMBL:KQQ47129.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 156..343
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 853..948
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1058 AA; 116698 MW; 90248B60F3731CFE CRC64;
MSIEDSEASL PPAQPDAPVA EPPKPRKRAR NALILVLLVG ASFAVYFGVQ ESRTSALQAR
VFTDLAGKMT YKVQPGVSNA IRFPHDSPYD ERLGYSSLPD YIGRLSAREY KVSAQARMSP
KMLELAGHGI FPTYHEKTRT GLTIYDCRAQ QLYATSYPER IYDKFEQTPM ALISTLLYIE
NRELLDNTYP KRNPAVEWDR LAKAVLEKSM SALGAGHRAA GGSTLATQIE KYRHSPEGRT
GSMTDKLQQM ISGSLRAYQD GPDTTKARRR IVIEYLNTVP LSAKPGYGEV NGVGDGMWVW
YGRSFDDFNR IMARNLEQPD ADTALVYKEA LSLMIAQRRP SYYLGDGAED LDQLADSHLR
ILAKDGVITA AMRDMALKQK LHPAKGNGLQ AAPPMTFVSR KATNAMRNHL ANLLGDNRMY
NLDRLDLDVT STLDAQAQTA VTQVLNDLRD PERAKAAGLT GKGMLGNGDP ANVVYSFTLL
EKGKDTNFLR LQTDNYDQPL DINEGAKLDL GSTAKLRTLV SYLDIMDQLH KKYAAMGAAE
LGKVVVDPQD RLSLWAIDYF KALPVDSAAR GLTPMLHAAM ERKYSGNPGE GFFTGGGLHY
FGNFSKEDNN KILTVTEALR HSTNLVFVRL MRDVAKFYMF QTPGSSASLL ADADDPRRAQ
YLARFADKEG KEFMARFWAK YKGKPVAEFD NILLANLRRT PVRLAVIHRT VYPKATEQEF
ASFLRANLSS QNEVSDERVA KLYDQYAIDQ WSLADRGYLA SVHPLELWMV AYLHANPGAT
LTQMNAASEK ERQDVYQWLL KTKRKHAQDR RIAGLLEVEG FMEVHKQWKK MGYPFDSLVP
SYATTLGASA DRPAALAELM GIIVNGGVRK TTQRVTSLHF AKQTPYETMI TRAKPVNNEQ
VLAPEVAQVV AEAIRGVVSD GTAKRARGAF TTSDGTPLPV GGKTGTGDQR FDVYGGGGRL
IESRYVNRSA TFVFNIGERF FGSMTAYVHG PESKNYDFTS ALPVQLLVVL APHLMPLIDP
HPVAKPAAAA AVVPGTAPEV AATLPKPVAP APLRACGG
//
