ID Q3AVA3_SYNS9 Unreviewed; 608 AA.
AC Q3AVA3;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Peptidoglycan glycosyltransferase {ECO:0000313|EMBL:ABB26612.1};
DE EC=2.4.1.129 {ECO:0000313|EMBL:ABB26612.1};
GN OrderedLocusNames=Syncc9902_1654 {ECO:0000313|EMBL:ABB26612.1};
OS Synechococcus sp. (strain CC9902).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=316279 {ECO:0000313|EMBL:ABB26612.1, ECO:0000313|Proteomes:UP000002712};
RN [1] {ECO:0000313|Proteomes:UP000002712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9902 {ECO:0000313|Proteomes:UP000002712};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9902.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000097; ABB26612.1; -; Genomic_DNA.
DR RefSeq; WP_011360423.1; NC_007513.1.
DR AlphaFoldDB; Q3AVA3; -.
DR STRING; 316279.Syncc9902_1654; -.
DR KEGG; sye:Syncc9902_1654; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_6_2_3; -.
DR OrthoDB; 9770103at2; -.
DR Proteomes; UP000002712; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.450.330; -; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF1; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE FTSI; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000313|EMBL:ABB26612.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:ABB26612.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 83..214
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 278..585
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 608 AA; 66941 MW; 9A3A876F78D9334D CRC64;
MARRSRPEQR SRRPSRTSTN RTRSRVVSLA PVPPKRLWIV FLILCTGLAG LVGRMAWLQL
VQAPVLEEQA RQLQTQRTRP LGQRRPIVDR TGRLVAIDEK RFRLWAHPRY FNLPGDPPNL
VRPPSDVVEL LAPHLAIPAS ELLIALRTRS SGIKLGEELD PETAKRIQAL GISGLDLEAY
PQRIYPQASL FANVVGFLNA ERVPQAGLEQ SRDSDLVRHE QTRSLRRGAD GTPLPDNLAP
GVFYGDDLRL QLTLDSRLQE LAVKALAAQV AQWKAKKGAA IVMDVTNGEL LVLASTPTYN
PNQYWSFPTG LFREWSVQDL YEPGSTFKPI NLALALQEKA IQPDDRVHDI GQLMVGGWPI
NNHDKKANGL IDFAKVLQVS SNVGMVQAMR QLDDQLYWTW MHRLGIDRRP DTDLPGAVAG
QLKTKEQFMT QPIEPATTAF GQGFSLTPLK LVQLHGMLAN DGRLVSPHIT RGFRSGAALA
PAAPPSGQQL LRPEVTRTVL QWMESVVDQG SGKGVQTPGY RIGGKTGTAQ KALNGIYLPG
AKICSFVATL PIEDPRYVVF VAVDEPQGAH AYGSTVAVPV AKQIIDALLV VERIAPSKPV
DLNKPTKS
//
