ID A0A0D0LXA4_9FLAO Unreviewed; 767 AA.
AC A0A0D0LXA4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=RT99_04655 {ECO:0000313|EMBL:KIQ23159.1};
OS Flavobacterium sp. MEB061.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1587524 {ECO:0000313|EMBL:KIQ23159.1, ECO:0000313|Proteomes:UP000032091};
RN [1] {ECO:0000313|EMBL:KIQ23159.1, ECO:0000313|Proteomes:UP000032091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MEB061 {ECO:0000313|EMBL:KIQ23159.1,
RC ECO:0000313|Proteomes:UP000032091};
RA Perisin M.A., Vetter M., Gilbert J.A., Bergelson J.;
RT "16Stimator: statistical estimation of ribosomal gene copy numbers from
RT draft genome assemblies.";
RL Submitted (DEC-2014) 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 -!- 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:KIQ23159.1}.
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DR EMBL; JXQR01000009; KIQ23159.1; -; Genomic_DNA.
DR RefSeq; WP_042563575.1; NZ_JXQR01000009.1.
DR AlphaFoldDB; A0A0D0LXA4; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000032091; 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:0006508; P:proteolysis; 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; 2.
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:SF11; PENICILLIN-BINDING PROTEIN 1B; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 71..245
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 428..682
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 767 AA; 86825 MW; CF501AB02F823A53 CRC64;
MATKKNNQPN STKDINYYKK KFWRFFVYFL LGILAFFLFA SWGLFGSMPS FEDLENPDSN
LATEIISSDG VVIGKYFKTN RSQLKYSDLP KSLVEALVAT EDARFYEHSG IDGRGTLRAV
FTLGTNGGAS TLTQQLAKQL FHGEGSKFLP FRIVQKIKEW IIAIRLERQY TKNEILAMYC
NVYDFGNYSV GVSSAAQTYF SKDPKDLTMD ESAILVGMFK NSGLYNPVRN PQGVKNRRNV
VLAQMEKAKM ISTAEKERLQ ALPIALKFKL ESHREGTATY FREYLRDYMK KWMAENKKPD
GSDYDIYKDG LKIYTTIDSR MQQYAEEAVS AHMKNLQQQF FIEQKNNKNA PFVNITQAET
EKLMMQAMKN STRWAIMKDL DKSEDDIIAS FKVKTQMRIF TWKGERDTIM TPLDSIRYYK
HFLQSGLMAM EPQTGNIKAW VGGINYKYFQ YDHVGQGARQ VGSTFKPFVY ATAIEELNMS
PCDSILDGPF MIHKGRHHVT EDWEPRNSDN RYRGMVTLKQ GLANSINTVS AKLIDRVGPE
AVVELTHKLG VKTEIPAQPS IALGAVDITV EDMVAAYSTF ANQGVYVKPQ FLSRIENKSG
EVIYEPIPES HDVLNKDIAF AVIKLLQGVT ETGSGARLRT QGGGSGDNRW TGYPYMFKNP
IAGKTGTTQN QSDGWFMGMV PNLVTGVWVG CEDRSARFKS LTYGQGATAA LPVWAYFMKL
CYADKNLQIS KSEFERPANL SIKVDCYSAP KVKDTTTTEQ NTDEFEL
//
