ID A0A0D8ZU51_9CYAN Unreviewed; 769 AA.
AC A0A0D8ZU51;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=UH38_16170 {ECO:0000313|EMBL:KJH70766.1};
OS Aliterella atlantica CENA595.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Chroococcidiopsidales;
OC Aliterellaceae; Aliterella.
OX NCBI_TaxID=1618023 {ECO:0000313|EMBL:KJH70766.1, ECO:0000313|Proteomes:UP000032452};
RN [1] {ECO:0000313|EMBL:KJH70766.1, ECO:0000313|Proteomes:UP000032452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CENA595 {ECO:0000313|EMBL:KJH70766.1,
RC ECO:0000313|Proteomes:UP000032452};
RA Rigonato J., Alvarenga D.O., Branco L.H., Varani A.M., Brandini F.P.,
RA Fiore M.F.;
RT "Draft genome of a novel marine cyanobacterium (Chroococcales) isolated
RT from South Atlantic Ocean.";
RL Submitted (FEB-2015) 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:KJH70766.1}.
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DR EMBL; JYON01000018; KJH70766.1; -; Genomic_DNA.
DR RefSeq; WP_045055711.1; NZ_JYON01000018.1.
DR AlphaFoldDB; A0A0D8ZU51; -.
DR STRING; 1618023.UH38_16170; -.
DR PATRIC; fig|1618023.3.peg.274; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000032452; 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:0009252; P:peptidoglycan biosynthetic process; IEA:InterPro.
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; IPR011815; PBP_1c.
DR InterPro; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02073; PBP_1c; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR Pfam; PF06832; BiPBP_C; 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:UP000032452};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 67..233
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 315..570
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 665..749
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 769 AA; 85918 MW; 110264C12B95A627 CRC64;
MNKWARRKHS WVFKIGQITL VLVLIGLLVR LLPYMFPIYA NNLTQERQAI EFSDRQGLPL
GTLLTRDLEH TAVVPLNRVS SHFIHAIIAA EDKRFYQHGA LELRAIARSL VQAARVKKVV
SGASTITMQL ARMLDPKPRN LGNKLQEIWL SWRLFAGMNK HEILYAYVNR LTMGSNIYGV
EAAARIYFGV PASDLNLAQA SILAALPNDP TDLNPYTGWE KLKHRQAYVL GRMVKDGYIS
REMSDRALAE KITLQPRQQG IIAAPHFLFW LASQLPKNSS SQVKTTIDRP LQQFVEAQVR
QIVQNLAVYN AHHAAAIVIG NHSGEVLAYV GSPDYFSLTD TGRNDGVQAL RQPGSTLKPF
SYQLALENRV IHTNTVLADV PTHYAIPGAK LYSPRDYSES FQGPVRVRLA LANSLNVPAV
KVLEKVGVPT FLNRLHQLGF DQLKHPPEYY GLGLTLGSGE VSLWELARAY VTMARNGQAL
PLTVTSPHLP ISPSPHLPKS PTWALITDIL SDRHARARAF GVDSVLSLPF PAAVKTGTSS
DYRDTWTVGF TTDYTVATWV GNFDGEPMKQ VSGVMGAAPL WNRIMLHLHE HKEPADFAPP
ASLVQRPICA ISGLKPTPAC PTVVQEYFYP EDLPDYDRNL DTFYRVVNGE SRLDLPSEYN
EWLAMQQQSV TTDGLKIVSP RNGDRFLVYT NSQQRLELKL ATLPDKPVEW WINGERLANS
ASGAVFWALR PGNWTVEVKS GEMRDRVNFQ VEVAESQSSR RGFSIAPSR
//
