ID K9XB63_9CHRO Unreviewed; 782 AA.
AC K9XB63;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=Glo7428_1165 {ECO:0000313|EMBL:AFZ29738.1};
OS Gloeocapsa sp. PCC 7428.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Chroococcaceae; Gloeocapsa.
OX NCBI_TaxID=1173026 {ECO:0000313|EMBL:AFZ29738.1, ECO:0000313|Proteomes:UP000010476};
RN [1] {ECO:0000313|EMBL:AFZ29738.1, ECO:0000313|Proteomes:UP000010476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7428 {ECO:0000313|EMBL:AFZ29738.1,
RC ECO:0000313|Proteomes:UP000010476};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Gloeocapsa sp. PCC 7428.";
RL Submitted (JUN-2012) 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};
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DR EMBL; CP003646; AFZ29738.1; -; Genomic_DNA.
DR RefSeq; WP_015187614.1; NC_019745.1.
DR AlphaFoldDB; K9XB63; -.
DR STRING; 1173026.Glo7428_1165; -.
DR KEGG; glp:Glo7428_1165; -.
DR PATRIC; fig|1173026.3.peg.1229; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_4_1_3; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000010476; Chromosome.
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; 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 Glycosyltransferase {ECO:0000313|EMBL:AFZ29738.1};
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:UP000010476};
KW Transferase {ECO:0000313|EMBL:AFZ29738.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 67..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 113..286
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 379..609
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..729
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 782 AA; 87289 MW; C4E8E438E71EBF81 CRC64;
MPWFKEQDAI SNTESAKKSN PSRKQPPRQK QLPRRKVVQI LTQIKQLPRQ LVSPAINKQP
WHRRQSLWLV GVGGSAIALG GIAFSIEQSL PKTAELFTVV REGTLTIKAA DGTILQQSGP
ATREQLKLAE IPKPLVQAFI ASEDRRFYQH NGIDYQGIAR ATVSNLRSAN VVEGGSTITQ
QLARILFLNQ ERTLWRKLKE IRLAQKIEAN LTKEQILERY LNLVYLGEGA YGVADAASVY
FSKSVDQLTL PEMALIAGLA PAPSRYSPSV NLAAAQQRRN LVLQRMREDR VLSSETATAA
IATSIDINPS SPKRLEVTAP YFTSYIQKEL PKYVAPEVIE AGGLIVETTL NPKWQNAAET
AVINTVANNG RWQNFEQAAL VAINPRNGEI RALVGGKDFG KNQFNRVTQA QRQPGSTFKG
FVYTAAIATG LSPYKSYQDA PFVVEGYEPQ NYSREFRGWL TMRDALRSSI NTVAVKVMMD
VGFDPVIQLA RQMGIKSELR PMYSLALGSS EVNLLELTSA YGTLATQGMH VEPHGIRRIL
NRSGEVLYTT TPQPKRVLDS GSAAISTWML QNVVQAGTGR PASLNRPVAG KTGTSDESRD
LWFVGYIPQL VAGVWLGNDN NEPTWGNSGT AAATWRQFMM AAVEDMPVED FPERPNLTGR
KGSIKAQPIK PKRVSSVRRS RSRREFQESN SDFNNNRPRR RYRRSYQQEA TVPEPRRRSR
RDERPAATRR TRNAPTPTPQ TQERLRERLR NLRQSEPQTQ QPPSQTNSSQ STAGSYVVPT
KE
//
