ID C9LG36_9BACT Unreviewed; 849 AA.
AC C9LG36;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=GCWU000325_01176 {ECO:0000313|EMBL:EEX71644.1};
OS Alloprevotella tannerae ATCC 51259.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Alloprevotella.
OX NCBI_TaxID=626522 {ECO:0000313|EMBL:EEX71644.1, ECO:0000313|Proteomes:UP000003460};
RN [1] {ECO:0000313|EMBL:EEX71644.1, ECO:0000313|Proteomes:UP000003460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51259 {ECO:0000313|EMBL:EEX71644.1,
RC ECO:0000313|Proteomes:UP000003460};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) 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:EEX71644.1}.
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DR EMBL; ACIJ02000018; EEX71644.1; -; Genomic_DNA.
DR RefSeq; WP_006254951.1; NZ_GG700642.1.
DR AlphaFoldDB; C9LG36; -.
DR STRING; 626522.GCWU000325_01176; -.
DR GeneID; 84576174; -.
DR eggNOG; COG5009; Bacteria.
DR HOGENOM; CLU_006354_2_4_10; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000003460; 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:UP000003460};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 44..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 94..279
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 453..692
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 757..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..849
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 849 AA; 95327 MW; 1078C63007B85FA0 CRC64;
MQTKSHSLLG KIKSFFVRLK RGVHRFWAWY KHLYSGQPWW KKTIVGILSF FSLLLIYVIA
VMTNFLWLFG KSPSLSEIMH PKNPSASEIY SADGQMIGRY YNENRSPVPY DSINKVFFEA
LVATEDERFY EHHGIDYQGL AAAAKDALLG HPRGASTITQ QLVKNMFRVR TQYGTGLLGK
IPGVRILIMK SKEMIIATEI ELTNSKQDIL RMYANTVDFG SNSYGIKTAA KTYFNTTPSK
LKTEEAAVLV GMLKATNAFN PRINPKRSLA RRNTVLEKMC ARKFLTRQEC DSLKQLPIEL
KFTIEDPTDG LAPYFRQAVA DYLKKQLPDL DLYTDGVKVY TTLDAKMQQY AEEAVREQMK
VVQRNFDVHW RGLGEPWRDE EGKIIPRFIE DIAARSDAYK QLAARYPNNP DSVNYYLNKP
HKVKLFGYDG AKEEEMSTMD SIRFMVKFMH AGFISMEPNT GYVRAWVGDI DFDAWKYDKV
RSMRQPGSTF KLFVYSAAME SGLIPSDSRK DEYIQMEVYD KIKKKDVIWR PHNANGRFSN
ANIPLRAAFA RSINTIAVKV GQEVGIPRVI QTAKAMGIKS PLDDTPSLAL GSSDVNLMEM
VNAYGTIANE GVHVEPVLVT KVVDSDGKVL YENKTESSQA ISWRSAFFMQ KMLEAGMTDA
GGTSQSMRHY MSAPYWNKQI EVGGKTGTSN NHSDAWFICV TPALVSGAWV GGEYRSIHFR
TGALGQGSKT ALPIVGLFMQ KVLADPQLSP RYIKKFPLPK ETMNPNDYGG DYIGSPNTDA
DSGQGGSDSL SNASEDLFGN EEAESKPSES TAPPAEPAQE NVPAEDKKGK AGRHKDKKQP
VKDSEDLFN
//
