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Database: UniProt
Entry: A0A3R8QUG2_9FLAO
LinkDB: A0A3R8QUG2_9FLAO
Original site: A0A3R8QUG2_9FLAO 
ID   A0A3R8QUG2_9FLAO        Unreviewed;       210 AA.
AC   A0A3R8QUG2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 12.
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};
GN   Name=rlpA {ECO:0000256|HAMAP-Rule:MF_02071};
GN   ORFNames=EIG84_05420 {ECO:0000313|EMBL:RRO19765.1};
OS   Flavobacteriaceae bacterium 14752.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=2491711 {ECO:0000313|EMBL:RRO19765.1, ECO:0000313|Proteomes:UP000274596};
RN   [1] {ECO:0000313|EMBL:RRO19765.1, ECO:0000313|Proteomes:UP000274596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=14752 {ECO:0000313|EMBL:RRO19765.1,
RC   ECO:0000313|Proteomes:UP000274596};
RA   Yu Y.;
RT   "Wangjiella luteus gen. nov., sp. nov., a novel bacterium of the family
RT   Flavobacteriaceae isolated from a saline lake.";
RL   Submitted (NOV-2018) 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:RRO19765.1}.
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DR   EMBL; RRZV01000048; RRO19765.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3R8QUG2; -.
DR   OrthoDB; 9779128at2; -.
DR   Proteomes; UP000274596; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008932; F:lytic endotransglycosylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
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   Gene3D; 3.30.70.1070; Sporulation related repeat; 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   InterPro; IPR007730; SPOR-like_dom.
DR   InterPro; IPR036680; SPOR-like_sf.
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   Pfam; PF05036; SPOR; 1.
DR   SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
DR   SUPFAM; SSF110997; Sporulation related repeat; 1.
DR   PROSITE; PS51724; SPOR; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_02071};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02071};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139}.
FT   DOMAIN          128..210
FT                   /note="SPOR"
FT                   /evidence="ECO:0000259|PROSITE:PS51724"
SQ   SEQUENCE   210 AA;  23779 MW;  DCD0C79A76FEE599 CRC64;
     MHKLLFILII FWGWPNQAQT QQGLASVRPL AHEGVMTKSG ERFSHDSLVA SHRSLPFGSV
     VKVTNSNNRQ SVEVKINDRG PFIKGRIIDL SERAANSIGV YKDNILRVRI DVLEIKQIFE
     PVTSSLTLNS EEKYIIQLAS YSKKENAINY TTELTKYKLK QPIQIQAQSI DGKALFKVFI
     GSFKTRDDAE KYKIQLPNAL QNGYVTTLKP
//
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