ID   A0A0C2QAE9_9CYAN        Unreviewed;       757 AA.
AC   A0A0C2QAE9;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, 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=SD81_10140 {ECO:0000313|EMBL:KIJ77123.1};
OS   Tolypothrix campylonemoides VB511288.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC   Tolypothrix.
OX   NCBI_TaxID=1245935 {ECO:0000313|EMBL:KIJ77123.1};
RN   [1] {ECO:0000313|EMBL:KIJ77123.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VB511288 {ECO:0000313|EMBL:KIJ77123.1};
RA   Tripathy S., Das S., Gupta A., Malar M.C., Adhikary S.P.;
RT   "Draft whole genome shotgun sequence of Tolypothrix campylonemoides
RT   VB511288.";
RL   Submitted (JAN-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:KIJ77123.1}.
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DR   EMBL; JXCB01000007; KIJ77123.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2QAE9; -.
DR   OrthoDB; 499624at2; -.
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   CDD; cd00060; FHA; 1.
DR   Gene3D; 2.60.200.20; -; 1.
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; IPR000253; FHA_dom.
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   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF00912; Transgly; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SMART; SM00240; FHA; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
FT   DOMAIN          64..118
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
SQ   SEQUENCE   757 AA;  83405 MW;  F52F740956104689 CRC64;
     MSSPQPPQKP QTLLGQITQA VQTIQARVDF SKLALKPNAK VPELWVQDAG ADKAEVYPLL
     GDRYIIGRSS KSCDIVVRNP VVSQIHLSLA RDSTQRQPVF VIKDENSTNG IYRGKRRLTS
     LELRHGDILT LGPPELAASV RLQYVDPPPW YVTAGTWAGY GVGGITTLMA LVIGVEWLKF
     DVKPLPGPTR APVVIYARDA TTKLREPRTT AHIDMKRLQD FGPYLPAAIV ASEDSRYYWH
     FGVDPLGILR AVFINTQSGD VQQGASTVTQ QVARSLFRDY VGRQDSLGRK FREAMVALKL
     ETFYSKDYIL LTYLNRVFLG ADTSGFEDAA RYYFDKSAKE LTLSEAATLV AILPAPNGFD
     YCTRGDSQNN LRTIEYRNRV LKRMLEMGKI KQDEYNRSRR SPIEISPKVC ERQAKTIAPY
     FYSYVFQELE NILGKELATE GNFIIETQLD PAIQAQAEVA LRNHVRTGKS SFNFSQGAML
     TLDSSNGAIL AMVGGTDYRT SQFNRAVQAK RQPGSTFKIF AYTAAIEQGI SPEKSYSCAP
     YRWQGFTYKP CRTGGGSLDI ARGLALSENP IALRVAHEVG LDKVVAMARE LGVKSQLEAV
     PGLVLGQSVV TVMEMTGAFG AIGNGGVWNR PHAISRILDS SDCRDRNDPK TCRVIYSYDQ
     DAEANKRVLQ TNIADTMTRL LRGVVTSGTG RSAAIGLGEA GKTGTTDKNV DLWFIGFVPG
     KRLVTGIWLG NDNNAPTSGS SAQAAQLWGN YMGKITR
//