ID A0A1B6YDW4_9BACT Unreviewed; 782 AA.
AC A0A1B6YDW4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=A8B79_13880 {ECO:0000313|EMBL:OAN64421.1};
OS Balneola sp. EhC07.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae; Balneola.
OX NCBI_TaxID=1849360 {ECO:0000313|EMBL:OAN64421.1, ECO:0000313|Proteomes:UP000078514};
RN [1] {ECO:0000313|EMBL:OAN64421.1, ECO:0000313|Proteomes:UP000078514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EhC08 {ECO:0000313|EMBL:OAN64421.1,
RC ECO:0000313|Proteomes:UP000078514};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) 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:OAN64421.1}.
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DR EMBL; LXYG01000002; OAN64421.1; -; Genomic_DNA.
DR RefSeq; WP_066217482.1; NZ_LXYG01000002.1.
DR AlphaFoldDB; A0A1B6YDW4; -.
DR STRING; 1849360.A8B79_13880; -.
DR InParanoid; A0A1B6YDW4; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000078514; 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 Reference proteome {ECO:0000313|Proteomes:UP000078514};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 52..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 102..274
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 436..696
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 782 AA; 88998 MW; 45346E4F0AD4F721 CRC64;
MSDKKEPIDH QRYFNDPEYR KEVLAERKAR EENSEEPSSK YGFSSDNLRK KIITWTGAVA
ATLLVVVIGY VIFLFQGLPP LEKLENPDTA IATEVRSRDG VVLDKYFTEN RTWVPYDQIS
PHVINALVAT EDHRFYNHWG IDMVRTLAIP FNLMRGRVEG GSTLSQQLAR NLYKEIGLKF
SISRKFREMI TAVQIEQNYT KREIIEMYLN TVEYANSAFG IEAASRTHYN KPAKELTLSE
SAVLVGSVNA VYAYNPRIYP ERSQRRRNIV LYLMNNQGFI DSTSYNQLKQ EPITLDYQPP
SKAGRVSRYF GEYVRQRVSG WAEENGYDIY KDGLVIYTTI DSRLQKHAER ALSTKLDSLQ
KIFEYEWTSR GSNEYMDKLW DEFPTFKDSF LEETDRYKNG YQTYNTKIRK VVLDSLKADT
AFVDSVLKAR TRLEASFVAI EPTNGNILAW VGGSNYGSVQ FDHVYQSRRQ VGSTFKPFVY
SVAIDNGFKP YHKFSKFPIS FRDRNGKVWN PKDAEVASGP NEVPLREALA RSMNNVTVRL
LPELAGYPGT NKLWELDAAA RKIKDMASNL GVDMSRTPAY PSIALGTAEA SLLEMTSAYT
TFANNGVHIE PIAITRIEDK EGNVLQEYFP EYRKEVISPE TAYMMVDMMR GVIRGGDGYF
GTGVRLRNVY GIRQDIAGKT GTTNDASDNW FIGMTPHIVM GAWVGGEDRR IRFPQDGSYS
IGQGARTALP IVGTFINYVT DDPEAYWGYD AFSPPPGFVM PEDPKEVRDE LGTDKNRGRI
GW
//
