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Database: UniProt
Entry: A0A5C8ZBR0_9GAMM
LinkDB: A0A5C8ZBR0_9GAMM
Original site: A0A5C8ZBR0_9GAMM 
ID   A0A5C8ZBR0_9GAMM        Unreviewed;       376 AA.
AC   A0A5C8ZBR0;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Peptidoglycan glycosyltransferase MrdB {ECO:0000256|HAMAP-Rule:MF_02079};
DE            Short=PGT {ECO:0000256|HAMAP-Rule:MF_02079};
DE            EC=2.4.1.129 {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   ECO:0000313|EMBL:TXR54250.1};
GN   Synonyms=mrdB {ECO:0000256|HAMAP-Rule:MF_02079};
GN   ORFNames=FME95_06860 {ECO:0000313|EMBL:TXR54250.1};
OS   Reinekea thalattae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Saccharospirillaceae; Reinekea.
OX   NCBI_TaxID=2593301 {ECO:0000313|EMBL:TXR54250.1, ECO:0000313|Proteomes:UP000321764};
RN   [1] {ECO:0000313|EMBL:TXR54250.1, ECO:0000313|Proteomes:UP000321764}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSH23 {ECO:0000313|EMBL:TXR54250.1,
RC   ECO:0000313|Proteomes:UP000321764};
RA   Kim I.;
RT   "Reinekea sp. strain SSH23 genome sequencing and assembly.";
RL   Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
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=2.4.1.129; 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 inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_02079}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_02079}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC       membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the SEDS family. MrdB/RodA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02079}.
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:TXR54250.1}.
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DR   EMBL; VKAD01000001; TXR54250.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5C8ZBR0; -.
DR   OrthoDB; 9768187at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000321764; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051301; P:cell division; IEA:InterPro.
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; IEA:UniProtKB-KW.
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 inner membrane {ECO:0000256|HAMAP-Rule:MF_02079};
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|HAMAP-Rule:MF_02079};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02079};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW   Rule:MF_02079}; Reference proteome {ECO:0000313|Proteomes:UP000321764};
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        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        88..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        151..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        173..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        195..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        274..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        312..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
FT   TRANSMEM        351..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02079"
SQ   SEQUENCE   376 AA;  41114 MW;  56D3BAC297AEF58B CRC64;
     MLNDFVRYDQ SGAFSQGRTL LQRLHIDIYL FMALLLVAMA GLIILYSATG GDLGAVSRQM
     VRFGVGFLAM FIVAQFDPRF FQQWSGVLYG VGLLLLLAVL YAGAHAKGAQ RWLDIFGLFR
     FQPSELVKVT VPIMLAWYLA RRGMPPKFRH ILLALIILFV PTVLIVMQPD LGTSVLIAAS
     GVFVIFLAGL SWKLIASAVV LALGSLPAMW LFVLHDYQKQ RVLTFLNPES DPLGAGWNII
     QSKTAIGSGG LYGKGYLHGT QSQLDFLPES HTDFIIAVLS EELGLIGVVA LLVCYFLIIW
     RGSYIAINAR DSFCRLLAGA LTLTFFIYVF VNIGMVSGLL PVVGVPLPLV SYGGTSIVSL
     LGSFGILMSI STHKRT
//
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