ID I2BB99_SHIBC Unreviewed; 371 AA.
AC I2BB99; K6UP99;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
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 ECO:0000313|EMBL:AFJ47803.1};
GN OrderedLocusNames=EBL_c27320 {ECO:0000313|EMBL:AFJ47803.1};
OS Shimwellia blattae (strain ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 /
OS CDC 9005-74) (Escherichia blattae).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shimwellia.
OX NCBI_TaxID=630626 {ECO:0000313|EMBL:AFJ47803.1, ECO:0000313|Proteomes:UP000001955};
RN [1] {ECO:0000313|EMBL:AFJ47803.1, ECO:0000313|Proteomes:UP000001955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 / CDC 9005-74
RC {ECO:0000313|Proteomes:UP000001955};
RX PubMed=22843577; DOI=10.1128/JB.00829-12;
RA Brzuszkiewicz E., Waschkowitz T., Wiezer A., Daniel R.;
RT "Complete genome sequence of the B12-producing Shimwellia blattae strain
RT DSM 4481, isolated from a cockroach.";
RL J. Bacteriol. 194:4436-4436(2012).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_02071};
CC Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_02071}.
CC -!- SIMILARITY: Belongs to the RlpA family. {ECO:0000256|HAMAP-
CC Rule:MF_02071, ECO:0000256|RuleBase:RU003495}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001560; AFJ47803.1; -; Genomic_DNA.
DR RefSeq; WP_002439198.1; NZ_BAHA01000001.1.
DR AlphaFoldDB; I2BB99; -.
DR STRING; 630626.EBL_c27320; -.
DR KEGG; ebt:EBL_c27320; -.
DR PATRIC; fig|630626.3.peg.2647; -.
DR eggNOG; COG0797; Bacteria.
DR HOGENOM; CLU_042923_3_0_6; -.
DR OrthoDB; 9779128at2; -.
DR Proteomes; UP000001955; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51724; SPOR; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_02071};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_02071};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|HAMAP-
KW Rule:MF_02071};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02071};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02071};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|HAMAP-Rule:MF_02071};
KW Reference proteome {ECO:0000313|Proteomes:UP000001955}.
FT DOMAIN 292..368
FT /note="SPOR"
FT /evidence="ECO:0000259|PROSITE:PS51724"
FT REGION 199..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 371 AA; 38253 MW; 451101B8965BE252 CRC64;
MRKQWLGVCV AAGLLAACST NDDGQQQVAP QPEPVVCNGP SVEISGADPR YEPLSPSANQ
DYQRNGKNYK IVQNPGQFTQ SGLAAIYDAE PGSNLAASGE PFDPGQLTAA HPTLPIPSYA
RITNLANGRM IVVRINDRGP YGNDRVISLS RASADRLNTS NNTKVKIDPI IVSQDGALSG
PGMACVTVAK QTYALPSRPD LSGGMGSASS APQLTPPQGE VRAISNDTLS ASDTTGAPVS
SSGFLGAPSA LHDGVVENSQ PATTAPQGQP VTAPVTAPGS VQGSVTAPAT ASAGNGEFLV
QVGAVSDAGR ASQWQQKLSQ QFGVPGRVTH NGVVYRVQMG PFASKSEAIA LQQRLLNEAQ
QQSFVTAATP Q
//
