ID Q2JMV3_SYNJB Unreviewed; 784 AA.
AC Q2JMV3;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN OrderedLocusNames=CYB_0950 {ECO:0000313|EMBL:ABD01929.1};
OS Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS Yellowstone B-Prime).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=321332 {ECO:0000313|EMBL:ABD01929.1, ECO:0000313|Proteomes:UP000001938};
RN [1] {ECO:0000313|EMBL:ABD01929.1, ECO:0000313|Proteomes:UP000001938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-2-3B'a(2-13) {ECO:0000313|Proteomes:UP000001938};
RX PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA Bhaya D., Grossman A.R., Steunou A.S., Khuri N., Cohan F.M., Hamamura N.,
RA Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT "Population level functional diversity in a microbial community revealed by
RT comparative genomic and metagenomic analyses.";
RL ISME J. 1:703-713(2007).
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; CP000240; ABD01929.1; -; Genomic_DNA.
DR RefSeq; WP_011432584.1; NC_007776.1.
DR AlphaFoldDB; Q2JMV3; -.
DR STRING; 321332.CYB_0950; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; cyb:CYB_0950; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_7_3; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000001938; Chromosome.
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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001938}.
FT DOMAIN 65..133
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
SQ SEQUENCE 784 AA; 86293 MW; 51035C39A0B8540F CRC64;
MSASEDKKPL LSTVARLFKT LARPFPVGPT ALLKPPEPPP PKRPVRLRIT CPGEPPQVVA
LKGSDILGRS QTVATIRIPA PAVSHLHAHI RPRPDWRLPG LGWRIPLPPI LYWLGWNAGR
YQLEDQDSTN GVFRLKPFGG VERVRRVILR HGQQLSLGPP WDPESIWIQV LDPPPPQVYG
VRGCLILIVV LGLGARIWIG HEWSKFSVEP PLSADRNPLI VLAGDQQTEL RRHQGDTYRE
LPNLEAFGPI LPKVVVAAED HRFYSHFGVD LLGIARAFWV NLRSGEVQQG GSSISQQLAR
TVLRDYTGSG NTFGRKLREA VAALKLEQRY SKDEILALYL NNVYLGNGIY GFETAAQFYF
GIPSRQLSLS EAATLAAILP APNAFNPVAN YDAAVRGRDR VLDRLSELKV FPEEEIRRAR
RSRLTLNPNL RSQTMTVAPY FYSAVFQELR QLLGQDLSAE GNFIIETTVH LPYQRLAEQV
LAQTVRESGS RLGFSQGALV SLDSRNGEVL ALVGGIDYNA SPFNRATQAQ RQPGSTFKVF
TYAAALTQGI PLSQVLSCEP LTWGNLTFRG CRSGSAPMDL ARGLILSENV IALRLAQQVG
LEQVVATARQ MGIQSPLQPY PSMVIGTMEV NLLELTAAFT PFANRGLWSR PHTIRRILDS
SDCANPNDFR TCREIYPGRE DPRSQRLVLP ETVAQQMTTV LQGVISSGTG TAARLGIGEA
GKTGTTTANK DLLFIGYTPN PPLVTGIWLG NDDSSPTRGS SSIAAQTWGN YTRQVITNSL
TMVQ
//
