ID Q73L35_TREDE Unreviewed; 261 AA.
AC Q73L35;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 94.
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 OrderedLocusNames=TDE_2030 {ECO:0000313|EMBL:AAS12544.1};
OS Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS / KCTC 15104).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=243275 {ECO:0000313|EMBL:AAS12544.1, ECO:0000313|Proteomes:UP000008212};
RN [1] {ECO:0000313|EMBL:AAS12544.1, ECO:0000313|Proteomes:UP000008212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104
RC {ECO:0000313|Proteomes:UP000008212};
RX PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA Seshadri R., Myers G.S., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA Ren Q., Brinkac L.M., Madupu R., Kolonay J., Durkin S.A., Daugherty S.C.,
RA Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G., Malek J.,
RA Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K., Pal S.,
RA Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E., Baca E.,
RA Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT "Comparison of the genome of the oral pathogen Treponema denticola with
RT other spirochete genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
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; AE017226; AAS12544.1; -; Genomic_DNA.
DR RefSeq; NP_972633.1; NC_002967.9.
DR RefSeq; WP_002679809.1; NC_002967.9.
DR AlphaFoldDB; Q73L35; -.
DR STRING; 243275.TDE_2030; -.
DR PaxDb; 243275-TDE_2030; -.
DR GeneID; 2740377; -.
DR KEGG; tde:TDE_2030; -.
DR PATRIC; fig|243275.7.peg.1915; -.
DR eggNOG; COG0797; Bacteria.
DR HOGENOM; CLU_042923_3_3_12; -.
DR OrthoDB; 9779128at2; -.
DR Proteomes; UP000008212; Chromosome.
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.
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, ECO:0000313|EMBL:AAS12544.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02071};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000008212}.
FT DOMAIN 29..115
FT /note="RlpA-like protein double-psi beta-barrel"
FT /evidence="ECO:0000259|Pfam:PF03330"
FT DOMAIN 190..231
FT /note="SPOR"
FT /evidence="ECO:0000259|Pfam:PF05036"
FT REGION 123..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 261 AA; 29633 MW; 3DF18DB879C248AB CRC64;
MKKTILMLIL FLSFMLFLTA QGEIISEETY ASYYGEAFNG RPTANGEIFD MNAYTAAHKT
LPFGTLVEVT NLENGRKVIV RINDRGPFVG NREIDVSKAA AAALDMLSYG VVRVSLRRID
PNNMGSFTST ETSEKPVNQE KTPVKTEETS SRAKDLVKTK EQDFQALTDS TKNKNLVYMP
AKASETEGVL WRIQLGSFKR EENALRLVIK LRKIGFEPAY EKTETTTRVV LYGIRPHELE
KVKRVLELNS FNDYVLRQES W
//
