ID A0A1I2V7K3_9BACT Unreviewed; 780 AA.
AC A0A1I2V7K3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SAMN05421739_10478 {ECO:0000313|EMBL:SFG85348.1};
OS Pontibacter chinhatensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=1436961 {ECO:0000313|EMBL:SFG85348.1, ECO:0000313|Proteomes:UP000198724};
RN [1] {ECO:0000313|EMBL:SFG85348.1, ECO:0000313|Proteomes:UP000198724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LP51 {ECO:0000313|EMBL:SFG85348.1,
RC ECO:0000313|Proteomes:UP000198724};
RA de Groot N.N.;
RL Submitted (OCT-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 ---------------------------------------------------------------------------
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; FOOT01000004; SFG85348.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2V7K3; -.
DR STRING; 1436961.SAMN05421739_10478; -.
DR Proteomes; UP000198724; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 80..265
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 442..687
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 780 AA; 88712 MW; 471B0FE42F4908F2 CRC64;
MLKMPKEQEK VQEPKKTSSS IASKVISFTW KIFFLGLFVI LGYLFSVEYN VLYLFGSSPS
LDRLENPRSD QASELYTADG KLIGKYFREN RSPVTYQELS PELVQALLAT EDIRFYEHAG
IDPEAIVSAV YGSFQGEARG ASTITQQLAK NLYKTRTDDS KGVLGHIPGL SIVISKTKEW
LTAIKLEQRY TKEEILTMYL NTVDFGSNSF GIKVASKTFF NTTPEKLKTE QAAVLVGLLK
APTYYSPRFN PENATRRRNV VMGQMVKYGY LDKAKADSLS QLPLVLDYSV ENHYDGPATY
FRGAVADYLQ EWCKENGYDL YRDGLKIYTT IDSRMQAHAE AAMEEQMRKL QRRFYSHWEG
KKPWVDEKNR EIPGFIEETI KRTAYYRRLK QKYGDDMEAI NKELNRPREM KVFTWDNDSL
EKTVTMSPLD SLAYYKHFLH GGMMTMDPFT GHIKAWVGGI NYKYFKYDHV KQARRQPGST
FKPFVYVAAI DNGYSPCDKI VDQRITINYV EKGEKKSWSP TNADWQYTGA PMTLRRGMGK
SVNSVTAQLT ELIGWETVVK YAHKLGIKSP LQAVPSIGLG PSDVSVFEMV GAYSTFPNYG
FHTEPMFITR IEDHNGNLLH QFTPIQKKVL SEETAFLMMH MLKGGIEEPG GTSQALWEYD
LWKGNEIGGK TGTSSNHSDG WFMGVTKDLV TGVWVGGEDR SIHFRTSQLG EGSKTALPIY
GLYMERIYQD EELGYTMGRF PKPTVKISKK YNCTTVLPKA QPDSTLLDPM LELLNIGDIL
//