ID   RLPA_NEIMB              Reviewed;         239 AA.
AC   Q9K1A0;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=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=NMB0267;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
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; AE002098; AAF40721.1; -; Genomic_DNA.
DR   PIR; D81218; D81218.
DR   RefSeq; NP_273323.1; NC_003112.2.
DR   RefSeq; WP_002221924.1; NC_003112.2.
DR   AlphaFoldDB; Q9K1A0; -.
DR   SMR; Q9K1A0; -.
DR   STRING; 122586.NMB0267; -.
DR   PaxDb; Q9K1A0; -.
DR   DNASU; 902378; -.
DR   EnsemblBacteria; AAF40721; AAF40721; NMB0267.
DR   KEGG; nme:NMB0267; -.
DR   PATRIC; fig|122586.8.peg.332; -.
DR   HOGENOM; CLU_042923_3_4_4; -.
DR   OMA; PYSALGM; -.
DR   Proteomes; UP000000425; 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: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   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   InterPro; IPR007730; SPOR-like_dom.
DR   Pfam; PF03330; DPBB_1; 1.
DR   Pfam; PF05036; SPOR; 1.
DR   SUPFAM; SSF50685; SSF50685; 1.
DR   TIGRFAMs; TIGR00413; rlpA; 1.
DR   PROSITE; PS51724; SPOR; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Lyase; Reference proteome; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT   CHAIN           26..239
FT                   /note="Endolytic peptidoglycan transglycosylase RlpA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT                   /id="PRO_0000030807"
FT   DOMAIN          160..239
FT                   /note="SPOR"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
SQ   SEQUENCE   239 AA;  25994 MW;  629EA8EFB7DF693A CRC64;
     MTLTRKTLFL LTAAFGTHSL QTASADAVVK AEKLHASANR SYKVAGKRYT PKNQVAEFTQ
     TGNASWYGGR FHGRKTSGGE RYDMNAFTAA HKTLPIPSYV RVTNTKNGKS VIVRVNDRGP
     FHGNRIIDVS KAAAQKLGFV NQGTAHVKIE QIVPGQSAPV AENKDIFIDL KSFGTEHEAQ
     AYLNQAAQNF AVSSSGTNLS VEKRRYEYVV KMGPFTSQER AAEAEAQARG MVRAVLTAG