ID F2BWK5_9FIRM Unreviewed; 688 AA.
AC F2BWK5;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=HMPREF9083_0572 {ECO:0000313|EMBL:EGF14872.1};
OS Dialister micraerophilus DSM 19965.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Dialister.
OX NCBI_TaxID=888062 {ECO:0000313|EMBL:EGF14872.1, ECO:0000313|Proteomes:UP000003503};
RN [1] {ECO:0000313|EMBL:EGF14872.1, ECO:0000313|Proteomes:UP000003503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19965 {ECO:0000313|EMBL:EGF14872.1,
RC ECO:0000313|Proteomes:UP000003503};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (FEB-2011) 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 -!- 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:EGF14872.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFBB01000009; EGF14872.1; -; Genomic_DNA.
DR RefSeq; WP_007555872.1; NZ_GL878519.1.
DR AlphaFoldDB; F2BWK5; -.
DR STRING; 888062.HMPREF9083_0572; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_2_9; -.
DR Proteomes; UP000003503; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase 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; 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 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:UP000003503};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 66..242
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 344..609
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 632..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 688 AA; 75134 MW; A477D5261884363A CRC64;
MKNSEIHRNR NKKKSVFGKF LKVIIIVCII ALAGIGAGLA FSLRGLPDVE SNMTPNISSR
IYDVKGRLIA TVHAEENRIP VPITEVPENL QNAFIAAEDV RFYEHHGIDP RGILRALFSN
IIHGQATGQG GSTITQQLAR NAFLSQEQTI KRKILEVFLA FEIESKYDKQ KILEMYMNQI
YFGQGCYGIE TASKVYFGKD SKDLTLAQCA MLAGLPNSPN YYSPFRSLEA AKSRQAVVLD
QMAKYGYITE EQAEAAKVAD VGLMKPSKVK SDVNKAPYFV NYVIQEISDK YDSEAIYKEG
LQIYTTLDLD MQEAAESAVR NDLPPGAKDK NGVSQPQAAL LSLEVGTGYV KAMVGGRGED
HFNRAVQMIR QPGSAFKPFV YAAALDSGLS PSTTLSNEKK EYAGGWVPKN YGGTYGGKVS
MIEALVHSMN VPTIDLANKV GMSKILKLAE SCGISTLVKD GKYSDNNLAA SIGGLTNGVS
VIDMAKAYSV FANDGVLVEP RAIIKVVDKN GNTLEDHSEK PQGKHILDQT TADKLTSMLE
QVITKGTGGG AYIGGAAAGK TGTTDDEHDA WFAGYTPHLS TVVWIGDDTS TNAGYTGGTV
PAVIWKDYMR VAEGIYPSKG FEISDNIRQQ TQYMSQKEKD EKEKKEKEEK DKKQKLQQTV
DKAKLNVKRA GEKLLDKIAG KGSQEDSE
//
