ID A0A1M5A129_9BURK Unreviewed; 300 AA.
AC A0A1M5A129;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-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};
GN Name=rlpA {ECO:0000256|HAMAP-Rule:MF_02071};
GN ORFNames=SAMN02745117_01568 {ECO:0000313|EMBL:SHF23999.1};
OS Lampropedia hyalina DSM 16112.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Lampropedia.
OX NCBI_TaxID=1122156 {ECO:0000313|EMBL:SHF23999.1, ECO:0000313|Proteomes:UP000184327};
RN [1] {ECO:0000313|EMBL:SHF23999.1, ECO:0000313|Proteomes:UP000184327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16112 {ECO:0000313|EMBL:SHF23999.1,
RC ECO:0000313|Proteomes:UP000184327};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FQUZ01000016; SHF23999.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M5A129; -.
DR STRING; 1122156.SAMN02745117_01568; -.
DR Proteomes; UP000184327; 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:SHF23999.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02071};
KW Reference proteome {ECO:0000313|Proteomes:UP000184327}.
FT DOMAIN 185..272
FT /note="RlpA-like protein double-psi beta-barrel"
FT /evidence="ECO:0000259|Pfam:PF03330"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 300 AA; 31520 MW; D0D2776FAB53001E CRC64;
MHTEDAYSQN GTKAVQGGGH GSGHWGIARM AMVAVLGWGL SACSVSVPDG RQALSTVTDA
TQPTAVEGKK APAPVPARQA VADDADDADD ADDAHVREET ALAPAVPQYS PLVQAALAQA
RLQSDRTLSI PSDLEPEARS TVSHLGLRSV EQERARTASP SAARAVSKAT AKASASLGLR
SDLLQTGRAS WYGDKFHGRM TANGERYNMN AMTAAHKTLP FGTQVCVRSL VSGNEVLVRI
NDRGPYAGNR IIDVSRGAAE KLGMIRLGLK EVALWIPSEE GGECGDGSVE IAGLRTKKSR
//
