ID I3DGD1_HAEPH Unreviewed; 201 AA.
AC I3DGD1;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=HMPREF1050_1135 {ECO:0000313|EMBL:EIJ70774.1};
OS Haemophilus parahaemolyticus HK385.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=1095744 {ECO:0000313|EMBL:EIJ70774.1, ECO:0000313|Proteomes:UP000003016};
RN [1] {ECO:0000313|EMBL:EIJ70774.1, ECO:0000313|Proteomes:UP000003016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK385 {ECO:0000313|EMBL:EIJ70774.1,
RC ECO:0000313|Proteomes:UP000003016};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (FEB-2012) 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:EIJ70774.1}.
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DR EMBL; AJSW01000028; EIJ70774.1; -; Genomic_DNA.
DR RefSeq; WP_005706421.1; NZ_UGHI01000002.1.
DR AlphaFoldDB; I3DGD1; -.
DR GeneID; 78224613; -.
DR PATRIC; fig|1095744.4.peg.1034; -.
DR OrthoDB; 9779128at2; -.
DR Proteomes; UP000003016; 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:EIJ70774.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02071};
KW Signal {ECO:0000256|HAMAP-Rule:MF_02071}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02071"
FT CHAIN 25..201
FT /note="Endolytic peptidoglycan transglycosylase RlpA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02071"
FT /id="PRO_5009991862"
FT DOMAIN 98..186
FT /note="RlpA-like protein double-psi beta-barrel"
FT /evidence="ECO:0000259|Pfam:PF03330"
FT REGION 60..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 201 AA; 22115 MW; 541E1C95D519E568 CRC64;
MRLSKIVTLL LAGFFTFGTL NSVAATKHAK TAIVSKQTKA QTPKKTLKDA SKAKFIKAEA
KKQSKAARQA VKSAKKHAKK PLSLTEKYKN TPRKHLQSGV ASYYADKFNG RRTANGERFD
NTAMTAAHPS LPFGTLIEVT NMRNGKKVVV RVNDRGPYTH ARVLDLSRNA ARQLGMHNTG
TAKVKVAVLD KNKRLELAEK S
//
