ID A0A2A2GRZ1_9GAMM Unreviewed; 325 AA.
AC A0A2A2GRZ1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-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=CBG25_19880 {ECO:0000313|EMBL:PAU99642.1};
OS Arsenophonus sp. ENCA.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Arsenophonus.
OX NCBI_TaxID=1987579 {ECO:0000313|EMBL:PAU99642.1, ECO:0000313|Proteomes:UP000217542};
RN [1] {ECO:0000313|EMBL:PAU99642.1, ECO:0000313|Proteomes:UP000217542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ENCA {ECO:0000313|EMBL:PAU99642.1};
RX PubMed=28854637; DOI=10.1093/gbe/evx134;
RA Mao M., Yang X., Poff K., Bennett G.;
RT "Comparative Genomics of the Dual-Obligate Symbionts from the Treehopper,
RT Entylia carinata (Hemiptera: Membracidae), Provide Insight into the Origins
RT and Evolution of an Ancient Symbiosis.";
RL Genome Biol. Evol. 9:1803-1815(2017).
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}.
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:PAU99642.1}.
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DR EMBL; NHNG01000786; PAU99642.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2GRZ1; -.
DR Proteomes; UP000217542; 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; IPR007730; SPOR-like_dom.
DR InterPro; IPR036680; SPOR-like_sf.
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; 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|HAMAP-Rule:MF_02071};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_02071};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000217542}.
FT DOMAIN 248..324
FT /note="SPOR"
FT /evidence="ECO:0000259|PROSITE:PS51724"
FT REGION 25..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 325 AA; 35402 MW; 5A51E55EF1CC3DE6 CRC64;
MHYHWLIFSI TIALLAGCVS QTKQHTNTPM APVQDISGAE PRYEPYHSGA NNDYQLNGQT
YQIVKDPAHF SETGFASIFG SEVIGKTTTT GEKASPYEFT ASHPTLPIPS YARITNLING
RMMIVRINDR GPYIAGKNIA LSQAAADRLN LMLTTRIKID PILVSPTGTL TGPGTIGVNI
TKQSYALPKP PKLETHSASS NQSTAENHTH QQPALSQSIQ STKIPSTVST NMVSQNNPAN
PSSMKSASVA TERYFVQIGA LSDQAKAAAW QQSVSKKLNT PGRIQPFNNI YRVQLGPFQN
SKIAEQIQNK ILIELNQSSI IINTE
//
