ID A0A1X7NT74_9RHOB Unreviewed; 722 AA.
AC A0A1X7NT74;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SAMN05661107_1180 {ECO:0000313|EMBL:SMH40971.1};
OS Maritimibacter sp. HL-12.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Maritimibacter.
OX NCBI_TaxID=1162418 {ECO:0000313|EMBL:SMH40971.1, ECO:0000313|Proteomes:UP000193836};
RN [1] {ECO:0000313|EMBL:SMH40971.1, ECO:0000313|Proteomes:UP000193836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-12 {ECO:0000313|EMBL:SMH40971.1,
RC ECO:0000313|Proteomes:UP000193836};
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; FXBQ01000001; SMH40971.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7NT74; -.
DR STRING; 1162418.SAMN05661107_1180; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000193836; 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:UP000193836};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 119..306
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 394..631
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..41
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 722 AA; 77362 MW; F10218208D7C5769 CRC64;
MAQKGSRRPP LVADKRYSGA SRGKKSAKKP PAKPPHKPRR PRRRRPFFIA WPLALLRWIF
RLGLRLAVVA TLVVGIMIGA GVFYFASTMP PLGQLVDGRA QGSVTLLDRH GEVFAWRGDQ
YGGLVTAETL SPHLRNAVIA TEDRRFYQHF GISPRGIASA MRINLAAGRG PLSGHGGSTL
TQQSAKLVCL GVPYDPASGM TEREYEADCR ETSLWRKIKE AVFALALEAK YSKNEILTIY
LNRAYLGAGS YGFEAASQRY FGKSASQINP SEAAVLAGLL TAPSTLAPTA NLQRSWDRAL
TVLRLMEEQG YLTAEEAADA RANPAELSAA AEARAGGNFA DWVMASGPSF LTRDTTEDVI
IRTTFDQAIQ KAAEEALAHV FETKVSPDSK AQAAIVVMSA DGAVRAMVGG RKIESSGTFN
RATQALRQTG SSFKPFVYGA ALDLGWRYDS LIEDAPFCMN IVGSGEWCPS NFDRKTRGWV
TLTDALRDSL NIPAVKLSEA VGRENVRTVA AMFGIESNLA LGPALALGAS ESTLLEMSGA
YAGILNGGSS VTPYGLVDLR LLGDNAPLME QAGGIGERVI TPQAAQALTY MMNQAVESGS
GQRARLDDRE VAGKTGTTSA ARDAWFLGFT ADYVAGVWMG YDDNTPLTGV TGGGLPAEIW
RETMVRVHQD MPPHPLPMIR PDAPPTAETG VPQPGGQGGT TRTPPGEDSL MGVLRSILGI
DR
//
