ID A0A1G6S9V7_PEPNI Unreviewed; 265 AA.
AC A0A1G6S9V7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=SAMN04489866_101268 {ECO:0000313|EMBL:SDD13461.1};
OS Peptococcus niger.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Peptococcus.
OX NCBI_TaxID=2741 {ECO:0000313|EMBL:SDD13461.1, ECO:0000313|Proteomes:UP000198995};
RN [1] {ECO:0000313|EMBL:SDD13461.1, ECO:0000313|Proteomes:UP000198995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20475 {ECO:0000313|EMBL:SDD13461.1,
RC ECO:0000313|Proteomes:UP000198995};
RA de Groot N.N.;
RL Submitted (OCT-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; FNAF01000001; SDD13461.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6S9V7; -.
DR STRING; 2741.SAMN04489866_101268; -.
DR Proteomes; UP000198995; 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; IPR012854; Cu_amine_oxidase-like_N.
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; PF07833; Cu_amine_oxidN1; 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:SDD13461.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02071};
KW Reference proteome {ECO:0000313|Proteomes:UP000198995};
KW Signal {ECO:0000256|HAMAP-Rule:MF_02071}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02071"
FT CHAIN 28..265
FT /note="Probable endolytic peptidoglycan transglycosylase
FT RlpA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02071"
FT /id="PRO_5011802989"
FT DOMAIN 44..130
FT /note="Copper amine oxidase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07833"
FT DOMAIN 172..260
FT /note="RlpA-like protein double-psi beta-barrel"
FT /evidence="ECO:0000259|Pfam:PF03330"
SQ SEQUENCE 265 AA; 28316 MW; 8BC3829100D6A4F7 CRC64;
MTKTIKSALA SFALGAFLLT SVGMAQAAEP ILWNQVDMIK TSGDLTYYPL RSVLEQTGVT
IKWVGNEART KLVLEAGGQS HQLILHADNQ TLTSGDQTFG YQNVNGSLML PLHFFMDVLD
QASVSTNRTT GALAITPVNQ DGKVGLRHLE AYVAEPKPQA PAAPAETCTY YQSGQATWYG
AALHGNYTAS GEPFNMYDLT AAHKTLPFGT RVKVTNLNNG LSVVVRITDR GPFAPGRVID
LSMAAAQQLN MISSGVAAVN LEIVG
//
