ID A0A433UJT0_ANAVA Unreviewed; 365 AA.
AC A0A433UJT0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=Probable endolytic peptidoglycan transglycosylase RlpA {ECO:0000256|HAMAP-Rule:MF_02071};
DE EC=4.2.2.- {ECO:0000256|HAMAP-Rule:MF_02071};
GN Name=rlpA {ECO:0000256|HAMAP-Rule:MF_02071};
GN ORFNames=DSM107003_40080 {ECO:0000313|EMBL:RUS94121.1};
OS Trichormus variabilis SAG 1403-4b.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC Trichormus.
OX NCBI_TaxID=447716 {ECO:0000313|EMBL:RUS94121.1, ECO:0000313|Proteomes:UP000276103};
RN [1] {ECO:0000313|EMBL:RUS94121.1, ECO:0000313|Proteomes:UP000276103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 1403-4b {ECO:0000313|EMBL:RUS94121.1,
RC ECO:0000313|Proteomes:UP000276103};
RX PubMed=30590650;
RA Will S.E., Henke P., Boedeker C., Huang S., Brinkmann H., Rohde M.,
RA Jarek M., Friedl T., Seufert S., Schumacher M., Overmann J.,
RA Neumann-Schaal M., Petersen J.;
RT "Day and night: Metabolic profiles and evolutionary relationships of six
RT axenic non-marine cyanobacteria.";
RL Genome Biol. Evol. 0:0-0(2018).
CC -!- FUNCTION: Lytic transglycosylase with a strong preference for naked
CC glycan strands that lack stem peptides. {ECO:0000256|HAMAP-
CC Rule:MF_02071}.
CC -!- SIMILARITY: Belongs to the RlpA family. {ECO:0000256|HAMAP-
CC Rule:MF_02071, ECO:0000256|RuleBase:RU003495}.
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:RUS94121.1}.
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DR EMBL; RSCM01000015; RUS94121.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A433UJT0; -.
DR OrthoDB; 9779128at2; -.
DR Proteomes; UP000276103; Unassembled WGS sequence.
DR GO; GO:0008932; F:lytic endotransglycosylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd22268; DPBB_RlpA-like; 1.
DR Gene3D; 2.40.40.10; RlpA-like domain; 1.
DR HAMAP; MF_02071; RlpA; 1.
DR InterPro; IPR034718; RlpA.
DR InterPro; IPR009009; RlpA-like_DPBB.
DR InterPro; IPR036908; RlpA-like_sf.
DR InterPro; IPR012997; RplA.
DR NCBIfam; TIGR00413; rlpA; 1.
DR PANTHER; PTHR34183; -; 1.
DR PANTHER; PTHR34183:SF1; ENDOLYTIC PEPTIDOGLYCAN TRANSGLYCOSYLASE RLPA; 1.
DR Pfam; PF03330; DPBB_1; 1.
DR SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_02071};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02071};
KW Reference proteome {ECO:0000313|Proteomes:UP000276103}.
FT DOMAIN 272..360
FT /note="RlpA-like protein double-psi beta-barrel"
FT /evidence="ECO:0000259|Pfam:PF03330"
SQ SEQUENCE 365 AA; 39095 MW; 037E3332DD5F4703 CRC64;
MNQRHLWTIV ALFLAVLGVP SVGRTQTIEG TSPANQALPT GDAVKVGEYQ SSTQKPASNT
VNAEIHPHSI GGRQAATLYI KNIPVLTFLS SAPVASTETK IGAIGNSEGL KYSTLVSTNS
KKVASFGNAI DVSNQISSID NDPVKRASVV ASRINQLIQE NVDASQITVS WKTENQSLVN
NKAQNKGDSV QQPDRYSIKV NDQELVEINQ GIQLADSTKN LAQDALQATN RLRRLIGNAS
PINEIANLPV TPVSLQKLPQ QIAIGGLKIN FKGIASWYGY DWSGNKTASG ERFNPEAFTA
AHRSLPMGTK VRVTNTRNGR SVVVRINDRG PYIGGRIIDL SAGAARILGM MSSGIAPVHI
EVLGR
//
