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Database: UniProt
Entry: A0A0F5Y8R6_9CYAN
LinkDB: A0A0F5Y8R6_9CYAN
Original site: A0A0F5Y8R6_9CYAN 
ID   A0A0F5Y8R6_9CYAN        Unreviewed;       642 AA.
AC   A0A0F5Y8R6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=WN50_29990 {ECO:0000313|EMBL:KKD34595.1};
OS   Limnoraphis robusta CS-951.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Sirenicapillariaceae; Limnoraphis.
OX   NCBI_TaxID=1637645 {ECO:0000313|EMBL:KKD34595.1, ECO:0000313|Proteomes:UP000033607};
RN   [1] {ECO:0000313|EMBL:KKD34595.1, ECO:0000313|Proteomes:UP000033607}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CS-951 {ECO:0000313|EMBL:KKD34595.1,
RC   ECO:0000313|Proteomes:UP000033607};
RA   Willis A., Parks M., Burford M.A.;
RT   "Draft genome assembly of filamentous brackish cyanobacterium Limnoraphis
RT   robusta strain CS-951.";
RL   Submitted (JUN-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:KKD34595.1}.
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DR   EMBL; LATL02000193; KKD34595.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F5Y8R6; -.
DR   PATRIC; fig|1637645.4.peg.3840; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000033607; 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; 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:SF35; 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   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:UP000033607};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        34..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          81..256
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          355..621
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   642 AA;  70126 MW;  C3486556356994CA CRC64;
     MSSTNAIHPK SRVNNSESIF DFVQSVSKVT AGTLLSVTML ASSVVAGGLV GLAVSFRNLP
     DVRVLQSYAP TETTYIYDIQ GRPLASLHDE ANREVISLDE ISPHLKRAVL AIEDSNFYYH
     KGIYPTGIIR AFVANLESGN TVEGGSTLTM QLVKNLFLSP NRTISRKAAE AVMAIRLEQI
     LAKDEILELY LNQVYWGHNL YGVETASRSY FNKSASDLTL AEASMLAGLI PAPEDYSPFV
     DYKKSKQRQL TVLQRMRELK WITAEEEAIA RKQPLLVGAI TSFKQSQLPY VTEAVVQELT
     RKFGRDAVLK GGMRVQTTID INFQRMAEQV VSTWHERLYY WGVYGSWDNG QIALAAVDPR
     THFVKAMVGG ADYKTSQYNR AIQAQRQPGS AFKPFVYYTA FATGKYSPES TVYDSPVSYP
     DGDGYYSPRN YGGGYSGAVS VRSALESSLN IPAVKLGQEV GLNQVIEVCR ILGFKSPMDP
     VISLPLGSVD VTPMEMAGGF ATFANNGWHS DPTFIVQVTD SQGNVLLDNT PKPRLVLNQW
     AVASLNSSLQ GVITGGTGTR AQIGRPAAGK TGTTSSERDV WFVGYTPQLS TAVWVGNDDY
     TPLASGSTGG TTVAPIWRDF MSRALSGQPG QGFPPPSNFE RP
//
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