ID A0A084TKE9_9FLAO Unreviewed; 777 AA.
AC A0A084TKE9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=IA57_04965 {ECO:0000313|EMBL:KFB01185.1};
OS Mangrovimonas yunxiaonensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Mangrovimonas.
OX NCBI_TaxID=1197477 {ECO:0000313|EMBL:KFB01185.1, ECO:0000313|Proteomes:UP000028521};
RN [1] {ECO:0000313|EMBL:KFB01185.1, ECO:0000313|Proteomes:UP000028521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LY01 {ECO:0000313|EMBL:KFB01185.1,
RC ECO:0000313|Proteomes:UP000028521};
RX PubMed=25428978;
RA Li Y., Zhu H., Li C., Zhang H., Chen Z., Zheng W., Xu H., Zheng T.;
RT "Draft Genome Sequence of the Algicidal Bacterium Mangrovimonas
RT yunxiaonensis Strain LY01.";
RL Genome Announc. 2:0-0(2014).
RN [2] {ECO:0000313|Proteomes:UP000028521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LY01 {ECO:0000313|Proteomes:UP000028521};
RA Li Y., Zheng T.;
RT "Genome sequence of Mangrovimonas yunxiaonensis.";
RL Submitted (JUL-2014) 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:KFB01185.1}.
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DR EMBL; JPFK01000005; KFB01185.1; -; Genomic_DNA.
DR RefSeq; WP_036120000.1; NZ_JPFK01000005.1.
DR AlphaFoldDB; A0A084TKE9; -.
DR STRING; 1197477.IA57_04965; -.
DR eggNOG; COG5009; Bacteria.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000028521; 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:UP000028521};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 68..246
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 433..690
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 757..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 777 AA; 87764 MW; 451BF70DC20D8012 CRC64;
MAKKKQVKQE HDFSTYVKWF WGLFLAGLVF IALLFLLARF EVFGDMPDHT VLENPKTNLA
TEVISADGQT LGKFYFNDNR TPVGYEDLPQ HLIDALIATE DARYYSHSGI DAWGTLRAVV
KMGSGGGAST ISQQLAKQLF HGEGSSNIAE RIIQKIKEWI IAIRLERQYT KEEIIAMYFN
IYDFGNNADG IRSASRIYFN KEPRDLNIKE SAMLVGMFKN SSLYNPRPHR NPIGTRNRRD
VVLSQMEKYG YINEAVKDSL QSTKLDLNYS PESHKEGVAT YFREFLRDFM KQWIEDNPKP
DGSKYNLYGD GLKVYTTIDS RMQQHAEYAV QQHMPRLQAE FDHQNTPQRN PTAPFLGLTQ
SEIDGLLKRS MKQSERWRHM KYDLKKSDEE IIKSFSQPTQ MTVFSWKGEI DTIMKPLDSM
RYYKSFLHPG MMSMDPQTGH VKVWVGGMNY KHFQYDHVKQ SKRQVGSTFK PFVYATAIDQ
LHLSPCDKLP NTQITIEAGK YGNTKAWTPK NAGGEYGGSI TLKSALANSV NTITARLMDK
VGPQPVVDLV KKLGVEAEIP VVPSIGLGSA DLSVYEMVAA YATFANQGVY NKPVMVTHIE
DKNGTILYQF KPESKDVLSA ETAYVTVNLL EGVTESGSGR RLRHKGADKW SAVYKEIITG
YPYELSNPIA GKTGTTQNQS DGWFMGMVPN LVTGVWVGAE DRAAHFRTIT YGQGASMALP
IWGMFMKSCY QDDQLNVSKG EFLKPQDLTI EVNCAKYDPE GQGDASPEED IPEELEF
//
