ID A0A1N7QCS8_9RHOB Unreviewed; 679 AA.
AC A0A1N7QCS8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-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=SAMN05421774_10915 {ECO:0000313|EMBL:SIT20576.1};
OS Gemmobacter megaterium.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Gemmobacter.
OX NCBI_TaxID=1086013 {ECO:0000313|EMBL:SIT20576.1, ECO:0000313|Proteomes:UP000186141};
RN [1] {ECO:0000313|EMBL:SIT20576.1, ECO:0000313|Proteomes:UP000186141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26375 {ECO:0000313|EMBL:SIT20576.1,
RC ECO:0000313|Proteomes:UP000186141};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-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; FTOT01000009; SIT20576.1; -; Genomic_DNA.
DR RefSeq; WP_076533646.1; NZ_FTOT01000009.1.
DR AlphaFoldDB; A0A1N7QCS8; -.
DR STRING; 1086013.SAMN05421774_10915; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000186141; Unassembled WGS sequence.
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; IPR011815; PBP_1c.
DR InterPro; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02073; PBP_1c; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR Pfam; PF06832; BiPBP_C; 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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000186141};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..679
FT /note="peptidoglycan glycosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009943964"
FT DOMAIN 58..224
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 302..523
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 596..675
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 679 AA; 71781 MW; 47F2CA9B89BF4A46 CRC64;
MIARGAFALA AGLWLAAVAR DGVDGWVAAT DLPPLTIPTG AEVVARDGRL LRAWTVADGR
WRLATDASRV DPLFLSMLVA YEDRRFATHP GVDLRAMVRA VAQAVWHGRV VSGGSTLTMQ
VARLLEESGT GRLSGKLRQI RVALALERRL TKGQILDLYL LLAPYGGNLE GVRAASLSWF
GREPTRLTPA QAALLVALPQ SPEARRPDRS QSAAAQGRAR VLARALAASL IDMDTATTAR
TEALPRSRQD FPRLAPHLTD RIRRGAPEQP RHATTVDADL QARLEALAAD AVRHHGARLQ
VALVVADHRS GEILASVGSA AYENDTRQGF VDMTQALRSP GSTLKPLVYA LAFDQGLAHP
ETLIEDRPIA FGRYQPQNFD RQFRGTVRVR AALQLSLNIP VVTLTEAIGP ERLMQGLRRA
GVDAVLPGGG PAGLAVSLGG VGVSLEHLTG LYAALARGGV ARPLSAVPEG GSEGERLISQ
VAAWQIGDIL AGLQPPDGTP SGRIAWKTGT SYGHRDAWAV GWDGRHVAGV WMGRADGTPV
PGAFGGDLAA PILFAALART SPRPSPLPPP PAATLQVENA RLPLPLQRFR PRGSIVAQGA
LPEIAFPPDG AEVALDGAPL LARVRGGTPP FTWMANGQPL DIGTSARESH LSLPGLGPLT
LSVIDANGQA SRVKVTLAH
//
