RLPA_TREPA
ID RLPA_TREPA Reviewed; 318 AA.
AC O83958;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Probable endolytic peptidoglycan transglycosylase RlpA {ECO:0000255|HAMAP-Rule:MF_02071};
DE EC=4.2.2.- {ECO:0000255|HAMAP-Rule:MF_02071};
DE Flags: Precursor;
GN Name=rlpA {ECO:0000255|HAMAP-Rule:MF_02071}; OrderedLocusNames=TP_0993;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
CC -!- FUNCTION: Lytic transglycosylase with a strong preference for naked
CC glycan strands that lack stem peptides. {ECO:0000255|HAMAP-
CC Rule:MF_02071}.
CC -!- SIMILARITY: Belongs to the RlpA family. {ECO:0000255|HAMAP-
CC Rule:MF_02071}.
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DR EMBL; AE000520; AAC65949.1; -; Genomic_DNA.
DR PIR; A71257; A71257.
DR RefSeq; WP_010882437.1; NC_000919.1.
DR AlphaFoldDB; O83958; -.
DR SMR; O83958; -.
DR IntAct; O83958; 284.
DR STRING; 243276.TPANIC_0993; -.
DR EnsemblBacteria; AAC65949; AAC65949; TP_0993.
DR KEGG; tpa:TP_0993; -.
DR eggNOG; COG0797; Bacteria.
DR HOGENOM; CLU_042923_3_3_12; -.
DR OMA; PANEDRK; -.
DR Proteomes; UP000000811; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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 Gene3D; 2.40.40.10; -; 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 Pfam; PF03330; DPBB_1; 1.
DR SUPFAM; SSF50685; SSF50685; 1.
DR TIGRFAMs; TIGR00413; rlpA; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Lyase; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT CHAIN 22..318
FT /note="Probable endolytic peptidoglycan transglycosylase
FT RlpA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT /id="PRO_0000030810"
FT REGION 121..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 318 AA; 33376 MW; 1597E8B85CC019F8 CRC64;
MMDKRVVAVA AVLWNVQMLF AAGEVIVPEG YASYYAESFN GRPTASGEIF DMNAYTAAHR
TLPFGTVVEL TNLDNGKKVI VRINDRGPYA ANREIDVSKA AAVALDMLNA GVARVSIHKA
DPNAHASQQR NDRQTSPGVL PQDSFGVPPT APTSSAPVMY ADPHNPPPAP VGRRAGTPGV
PGVANTTDVP ASEYGAPPVA YAAPGSTPSR VPYGTAVPGS AAPNSHAQPV PSSSSYAAAA
PLPYAAGGGK VSGMKSVYTP THSGETRGVL WRIQLGAFVR EENALRLVVK CARRALILHM
SEQSTRCAWC CRGYAPRT
