ID A3Z789_9SYNE Unreviewed; 709 AA.
AC A3Z789;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=RS9917_11825 {ECO:0000313|EMBL:EAQ69127.1};
OS Synechococcus sp. RS9917.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=221360 {ECO:0000313|EMBL:EAQ69127.1, ECO:0000313|Proteomes:UP000005593};
RN [1] {ECO:0000313|EMBL:EAQ69127.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS9917 {ECO:0000313|EMBL:EAQ69127.1};
RA Scanlan D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (JAN-2006) 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:EAQ69127.1}.
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DR EMBL; AANP01000003; EAQ69127.1; -; Genomic_DNA.
DR RefSeq; WP_007102314.1; NZ_CH724158.1.
DR AlphaFoldDB; A3Z789; -.
DR STRING; 221360.RS9917_11825; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_7_3; -.
DR Proteomes; UP000005593; 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 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 Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transferase {ECO:0000313|EMBL:EAQ69127.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 112..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 23..72
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
SQ SEQUENCE 709 AA; 76724 MW; 9D3CE498470B2809 CRC64;
MARLCIDQAG QPSQSIPLHG EAYRLGREEG MELSLDHPAV SRQHALLRRR GRRWVLEDLN
STNGLWWRGR RVQELELRDG DRISLAPASE PGAPCLRFLN PAEQGRRRLE RLLGFGLLTG
LGATAALMLI AVLDVPIRGR LATVQGPIAI YDRLNKPLES VDSSRHRELK TISAFSPALV
DALLSSEDNR FWWHPGVDPI GTLRAFATNL SGGRLIEGGS SLTQQLARSL YPDQVGQGDT
LGRKWRELLV ALQLESRFSK GELLLSYLNR VYLGVGWGFE DASRVYFNKS ASKLSLPEAA
LLVGLLPSPN GHDPCRYPQR ALEARNRVLN KMADAGRLSL EEARLARRQP IQLAKAACSK
ESLRRSAPFY TDQVRRDLSA LVGPDVAAEG NFLIETHLDP VLQQVVERQL QELLNQAQGL
GVGEGAAVVI DSRNGGVLAI AGGRDYRSSQ FNRATMALRQ PGSTFKLLTY LAALQRGIKP
GDGIDCSTLE WGGQRFESSC NGRLSLTSAF ASSSNTAALR LARRVGLEQV VRQARALGIN
TPLDPVPGLA LGQSEVRLIE LTGAYAAVAN DGLWHPPTTI RRLLDAESCS ADTLKRCGSL
TGDGSAQVSS ARRAISKDVA RRMQAMLRAV VRGGTGSAAS LGGLEGGKTG TTNDGRDLLF
IGYEPSRHWV LGIWLGNDDN SPTASSSALA ASLWGDIMRA AGRGSAGQR
//
