ID A0A1M5G0K4_9FLAO Unreviewed; 160 AA.
AC A0A1M5G0K4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 34.
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};
DE Flags: Precursor;
GN Name=rlpA {ECO:0000256|HAMAP-Rule:MF_02071};
GN ORFNames=SAMN05444396_103170 {ECO:0000313|EMBL:SHF96962.1};
OS Flavobacterium segetis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=271157 {ECO:0000313|EMBL:SHF96962.1, ECO:0000313|Proteomes:UP000184036};
RN [1] {ECO:0000313|Proteomes:UP000184036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19741 {ECO:0000313|Proteomes:UP000184036};
RA Varghese N., Submissions S.;
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; FQWE01000003; SHF96962.1; -; Genomic_DNA.
DR RefSeq; WP_072989154.1; NZ_FQWE01000003.1.
DR AlphaFoldDB; A0A1M5G0K4; -.
DR STRING; 271157.SAMN05444396_103170; -.
DR OrthoDB; 9779128at2; -.
DR Proteomes; UP000184036; 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:SHF96962.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02071};
KW Signal {ECO:0000256|HAMAP-Rule:MF_02071}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02071"
FT CHAIN 19..160
FT /note="Probable endolytic peptidoglycan transglycosylase
FT RlpA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02071"
FT /id="PRO_5013404819"
FT DOMAIN 66..147
FT /note="RlpA-like protein double-psi beta-barrel"
FT /evidence="ECO:0000259|Pfam:PF03330"
SQ SEQUENCE 160 AA; 17964 MW; 9F2C8E809FF96D52 CRC64;
MKKSLTLFLL LAAFTLMNSQ NLKTGSTKVS VQKDSVRKNK IIAEIQEKKT DSIIAVLEIF
KLYKKTVHAS YYADKFTGKK TASGVRFDNN KYTAAHKKLP FGTRVKVTNE KNGKWVVVEV
TDRGPFVKSR EIDLSKRAFM DIATNKGSGG ILVTMEIIEK
//
