ID A5HZF9_CLOBH Unreviewed; 386 AA. AC A5HZF9; A7G1B6; DT 26-JUN-2007, integrated into UniProtKB/TrEMBL. DT 26-JUN-2007, sequence version 1. DT 24-JUL-2024, entry version 96. DE RecName: Full=Peptidoglycan glycosyltransferase RodA {ECO:0000256|HAMAP-Rule:MF_02079}; DE Short=PGT {ECO:0000256|HAMAP-Rule:MF_02079}; DE EC=2.4.99.28 {ECO:0000256|HAMAP-Rule:MF_02079}; DE AltName: Full=Cell elongation protein RodA {ECO:0000256|HAMAP-Rule:MF_02079}; DE AltName: Full=Cell wall polymerase {ECO:0000256|HAMAP-Rule:MF_02079}; DE AltName: Full=Peptidoglycan polymerase {ECO:0000256|HAMAP-Rule:MF_02079}; DE Short=PG polymerase {ECO:0000256|HAMAP-Rule:MF_02079}; GN Name=rodA {ECO:0000256|HAMAP-Rule:MF_02079}; GN OrderedLocusNames=CBO0615 {ECO:0000313|EMBL:CAL82168.1}; OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=441771 {ECO:0000313|EMBL:CAL82168.1, ECO:0000313|Proteomes:UP000001986}; RN [1] {ECO:0000313|EMBL:CAL82168.1, ECO:0000313|Proteomes:UP000001986} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger] RC {ECO:0000313|Proteomes:UP000001986}; RX PubMed=17519437; DOI=10.1101/gr.6282807; RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G., RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L., RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M., RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A., RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S., RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M., RA White B., Whithead S., Parkhill J.; RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain RT Hall A and comparative analysis of the clostridial genomes."; RL Genome Res. 17:1082-1092(2007). CC -!- FUNCTION: Peptidoglycan polymerase that is essential for cell wall CC elongation. {ECO:0000256|HAMAP-Rule:MF_02079}. 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=2.4.99.28; Evidence={ECO:0000256|HAMAP- CC Rule:MF_02079}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_02079}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_02079}; CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_02079}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the SEDS family. MrdB/RodA subfamily. CC {ECO:0000256|HAMAP-Rule:MF_02079}. 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; AM412317; CAL82168.1; -; Genomic_DNA. DR RefSeq; WP_011948344.1; NC_009698.1. DR RefSeq; YP_001253157.1; NC_009495.1. DR RefSeq; YP_001386550.1; NC_009698.1. DR AlphaFoldDB; A5HZF9; -. DR GeneID; 5184870; -. DR KEGG; cbh:CLC_0670; -. DR KEGG; cbo:CBO0615; -. DR PATRIC; fig|413999.7.peg.614; -. DR HOGENOM; CLU_029243_0_1_9; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000001986; Chromosome. DR GO; GO:0032153; C:cell division site; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0015648; F:lipid-linked peptidoglycan transporter activity; IBA:GO_Central. DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0051301; P:cell division; IBA:GO_Central. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central. DR HAMAP; MF_02079; PGT_RodA; 1. DR InterPro; IPR018365; Cell_cycle_FtsW-rel_CS. DR InterPro; IPR001182; FtsW/RodA. DR InterPro; IPR011923; RodA/MrdB. DR NCBIfam; TIGR02210; rodA_shape; 1. DR PANTHER; PTHR30474; CELL CYCLE PROTEIN; 1. DR PANTHER; PTHR30474:SF1; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE MRDB; 1. DR Pfam; PF01098; FTSW_RODA_SPOVE; 1. DR PROSITE; PS00428; FTSW_RODA_SPOVE; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_02079}; KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP- KW Rule:MF_02079}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316, KW ECO:0000256|HAMAP-Rule:MF_02079}; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP- KW Rule:MF_02079}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02079}; KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02079}; KW Reference proteome {ECO:0000313|Proteomes:UP000001986}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_02079}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_02079}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_02079}. FT TRANSMEM 21..42 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079" FT TRANSMEM 54..74 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079" FT TRANSMEM 86..104 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079" FT TRANSMEM 116..139 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079" FT TRANSMEM 151..168 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079" FT TRANSMEM 174..190 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079" FT TRANSMEM 195..214 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079" FT TRANSMEM 283..303 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079" FT TRANSMEM 315..343 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079" FT TRANSMEM 349..372 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02079" SQ SEQUENCE 386 AA; 42949 MW; 5CA4B048786E16BC CRC64; MIRRKNVNLN KSFNLKRHIK YFDVFLFIVI ILISILGIVM ISSATSNFEN SRKYIITQIL SLVIGLVFMF ITIYIDYRNI GRAYKIIYIF NFLLLAGVIL LGTGKDQWGA QRWIRIGGIG IQPSEIAKIG FIITFAKFLE LIKDDLNKIK YLLAAFCYIG VPIILVMIQP DLGTALSFVF ISIAMIYICG IDYKYILGGF LACIVIIPIA WQYVLKAYQK NRILIFINPD SDPMGGGYHV LQSKIAVGSG EFFGTGLFKG SHAQNFLPEK HTDFIFALIG EELGFIGSII VVLLLLIIVL RCISIAKSAK DNLGCYICVG VASMIIFQTF INIGMCIGIM PVTGIPLPFI SYGGSSLITN FVAMGLVLNV GLRHKPINFF KGSINN //