ID A0A1Z4BZP1_9GAMM Unreviewed; 152 AA.
AC A0A1Z4BZP1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Endolytic peptidoglycan transglycosylase RlpA {ECO:0000256|HAMAP-Rule:MF_02071};
DE EC=4.2.2.- {ECO:0000256|HAMAP-Rule:MF_02071};
DE Flags: Precursor;
GN Name=rlpA {ECO:0000256|HAMAP-Rule:MF_02071};
GN ORFNames=CEK71_11950 {ECO:0000313|EMBL:ASF46730.1};
OS Methylovulum psychrotolerans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylovulum.
OX NCBI_TaxID=1704499 {ECO:0000313|EMBL:ASF46730.1, ECO:0000313|Proteomes:UP000197019};
RN [1] {ECO:0000313|EMBL:ASF46730.1, ECO:0000313|Proteomes:UP000197019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HV10_M2 {ECO:0000313|EMBL:ASF46730.1,
RC ECO:0000313|Proteomes:UP000197019};
RA Mateos-Rivera A.;
RT "Genome Sequencing of the methanotroph Methylovulum psychrotolerants str.
RT HV10-M2 isolated from a high-altitude environment.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
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; CP022129; ASF46730.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4BZP1; -.
DR KEGG; mpsy:CEK71_11950; -.
DR OrthoDB; 9779128at2; -.
DR Proteomes; UP000197019; Chromosome.
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 Lipoprotein {ECO:0000313|EMBL:ASF46730.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02071};
KW Reference proteome {ECO:0000313|Proteomes:UP000197019};
KW Signal {ECO:0000256|HAMAP-Rule:MF_02071}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02071"
FT CHAIN 25..152
FT /note="Endolytic peptidoglycan transglycosylase RlpA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02071"
FT /id="PRO_5013414592"
FT DOMAIN 58..145
FT /note="RlpA-like protein double-psi beta-barrel"
FT /evidence="ECO:0000259|Pfam:PF03330"
FT REGION 27..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..50
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 152 AA; 16807 MW; 4410888F5B3196A3 CRC64;
MNKLITAMLY LVVCSFFSNP ISTAAAAKHS GRHHQHHTAR HPHHYRHHHS GSRNGGNEGI
ASWYGNQFQG HVTASGERYD MNELTAAHNS LPLSSYVQVT NMHNQRTVVV RINDRGPYTG
NRVMDLSYAA AKELGIHKSG TAAIKITPLA MN
//