ID A3YVK1_9SYNE Unreviewed; 783 AA.
AC A3YVK1;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=WH5701_15141 {ECO:0000313|EMBL:EAQ76153.1};
OS Synechococcus sp. WH 5701.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=69042 {ECO:0000313|EMBL:EAQ76153.1, ECO:0000313|Proteomes:UP000002935};
RN [1] {ECO:0000313|EMBL:EAQ76153.1, ECO:0000313|Proteomes:UP000002935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH5701 {ECO:0000313|Proteomes:UP000002935};
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 (FEB-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:EAQ76153.1}.
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DR EMBL; AANO01000002; EAQ76153.1; -; Genomic_DNA.
DR RefSeq; WP_006171957.1; NZ_CH724159.1.
DR AlphaFoldDB; A3YVK1; -.
DR eggNOG; COG0744; Bacteria.
DR eggNOG; COG1716; Bacteria.
DR HOGENOM; CLU_006354_2_7_3; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000002935; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002935}.
FT DOMAIN 99..151
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 783 AA; 84047 MW; DBDC549623B9F1A5 CRC64;
MVERSAPERA CEQVSGSSTE SSTESSADLS TESSTEPRLA GGRRGAWRRL LSALSRGGPD
GRPAAIRSAW GQLLERQAVA ELWLGQRRVS RTVLGEGRYR IGRDPACELP IEAGSLSRVH
AILEKPRPRE RDFALEDFNS ANGLFHRDRR IRAIRLRHGD QVQLGSPLKG SAPRLRYLHP
RSPLEQAVHL LGLGSLLGSG LLVGGLLLAS SVGGGSRIRL ISGPVKIVSA SGQQIDAREG
SATALPSLQA YPLHLRQALL ASEEARFGWN SGVDLFGTLR SVLLGSGGGS GLTQQVARIY
YPEVGTDYSL SRKLRELWVA LQLEVGYSKN QILKMYLDRA HLGLGTDGFE QASRLYFRKS
ASDLDVGQAA FLVGLLPSPN GYSPCNTKDP TAGRERRDLV LKLMHEQGYL RDQQLIDAQR
RPLNIDPSAC RESSFSSYPF FSDYVLGELE GTRFGLNLSE KASGGNYYVV STIDPKLQQL
AQQQLQRFLE GPAARVGLTQ GALISLDFRS GKILAYVGGG DYSRSSFDRV QAMRQPGSTF
KLFPYLAALE AGTSLEQPIS CAPLAYVAGC RHGAAGGSIS VARGFADSEN VVALRLAESA
GLKQVVSKAR QLGISTPLDA DFNTMLGGRE TLLYEMARAY AVVANGGRSV PMHGVSKIYD
LGICRSIYSL ASCPERGVTT PIGEQPRQLL RGEDAAAMDE LLAGVVRSGT GRAAAAVADA
RGKTGTTDNG VDVLFIGYSP ALEILTAIWM GNDDNRPAQA ASGALVAELW GRYMAAIGAG
RQT
//
