ID G6XLS6_9PROT Unreviewed; 205 AA.
AC G6XLS6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=GMO_23250 {ECO:0000313|EMBL:EHH67330.1};
OS Gluconobacter morbifer G707.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=1088869 {ECO:0000313|EMBL:EHH67330.1, ECO:0000313|Proteomes:UP000004949};
RN [1] {ECO:0000313|EMBL:EHH67330.1, ECO:0000313|Proteomes:UP000004949}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G707 {ECO:0000313|EMBL:EHH67330.1,
RC ECO:0000313|Proteomes:UP000004949};
RA Lee W.-J., Kim E.-K.;
RT "Genome sequence of Gluconobacter morbifer G707, isolated from Drosophila
RT gut.";
RL Submitted (OCT-2011) 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 -!- 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:EHH67330.1}.
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DR EMBL; AGQV01000010; EHH67330.1; -; Genomic_DNA.
DR AlphaFoldDB; G6XLS6; -.
DR STRING; 1088869.GMO_23250; -.
DR PATRIC; fig|1088869.3.peg.2319; -.
DR eggNOG; COG0797; Bacteria.
DR Proteomes; UP000004949; 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 Lipoprotein {ECO:0000313|EMBL:EHH67330.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02071};
KW Reference proteome {ECO:0000313|Proteomes:UP000004949};
KW Signal {ECO:0000256|HAMAP-Rule:MF_02071}.
FT SIGNAL 1..37
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02071"
FT CHAIN 38..205
FT /note="Endolytic peptidoglycan transglycosylase RlpA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02071"
FT /id="PRO_5009991678"
FT DOMAIN 72..161
FT /note="RlpA-like protein double-psi beta-barrel"
FT /evidence="ECO:0000259|Pfam:PF03330"
FT REGION 175..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 205 AA; 21728 MW; 6D6CDBA118BFDD53 CRC64;
MPCKRPAFSS PFHWVSLRGL TFIVALAGMT GGSAARAADD SPDQSGGLVR TSWAASVRDA
LAHRAHEAAT WTQHGMASWY GRHFHGRRTS SGATFDTNAL TAAHPSLPLG TKLLVTSQDT
GRSVVVTVND RGPFNSRIID LSHAAAAKIG MLNSGTAHVT IARMEDVPAE TEVAEADPSD
TTAQAVQVAA SPQATAHTRR HRRRS
//
