ID A0A1Y6BAU4_9PROT Unreviewed; 717 AA.
AC A0A1Y6BAU4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SAMN05428998_101620 {ECO:0000313|EMBL:SME93868.1};
OS Tistlia consotensis USBA 355.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Fodinicurvataceae; Tistlia.
OX NCBI_TaxID=560819 {ECO:0000313|EMBL:SME93868.1, ECO:0000313|Proteomes:UP000192917};
RN [1] {ECO:0000313|EMBL:SME93868.1, ECO:0000313|Proteomes:UP000192917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USBA 355 {ECO:0000313|EMBL:SME93868.1,
RC ECO:0000313|Proteomes:UP000192917};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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}.
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DR EMBL; FWZX01000001; SME93868.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6BAU4; -.
DR STRING; 560819.SAMN05428998_101620; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000192917; 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:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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 NCBIfam; TIGR02074; PBP_1a_fam; 1.
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; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000192917};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 69..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 117..291
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 377..643
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 717 AA; 75837 MW; 76C8F70C717C8B50 CRC64;
MARRTAPRGT ATPALRADIE TSAAERRLRG AARSGSGGGR SAAARGGSGG GTGKRAAARP
RDWRWLRRLA LWTGVAAIWG AVALGGLLAW YAYDLPSVSA LGDYTRKPSI RLIDADGRPL
AAFGDLYGDT IPVADLPAYL PQAVMAVEDR RFYSHFGIDP WGILRALVAD VMAGQLREGG
STITQQLAKN LFLTPDRTIK RKVQEMMLAI WLETKLSKDR ILSLYLNRVY LGAGTYGVDA
AAHRYFGKSA REVGLYEAAM IAGLLKAPSR YNPANDPDLA HRRASTVLHS MAEAGFITEA
EAERAIRERK RGQPQVADRG RYFADWALSR VAEEAGPLEG DVVVSTTLDS RVQRIAEEET
AKLLDGAARK AGAGQAAVVV MGPDGAVKAM VGGRSYGDSQ FNRAVQALRQ PGSSFKPFVY
LAALESGMTP DSPVLDAPIE FKTPNGVWRP SNFTDKYRGT VTLREALARS LNTPAVRLAE
SVGVDKVAAV AHRMGITTPL AENLSLALGS SEVSVLDMAT AYSVLANGGD GVLPYGVSRI
ESADGQLIYD RHGGGLGRVI PPAVQASMVD MMQSAVAWGT ARHADPGRPA AAKTGTSQDF
RDAWFVGFTA DWTVAVWLGN DDGKPMDGVT GGSLPAQLWR AIMTRISAGL PPRPLVYAAA
VPSGAGRAGE APASDQGGGG PGLLENLIER LTGSGGGTAQ PRSDGAGRRL TKPGNDR
//
