ID   RLPA_NEIMA              Reviewed;         239 AA.
AC   Q9JSM7; A1IU42;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=NMA2219;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(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; AL157959; CAM09312.1; -; Genomic_DNA.
DR   PIR; F81795; F81795.
DR   RefSeq; WP_002245836.1; NC_003116.1.
DR   AlphaFoldDB; Q9JSM7; -.
DR   SMR; Q9JSM7; -.
DR   EnsemblBacteria; CAM09312; CAM09312; NMA2219.
DR   KEGG; nma:NMA2219; -.
DR   HOGENOM; CLU_042923_3_4_4; -.
DR   OMA; PYSALGM; -.
DR   BioCyc; NMEN122587:NMA_RS11305-MON; -.
DR   Proteomes; UP000000626; 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; 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_0000030806"
FT   DOMAIN          160..239
FT                   /note="SPOR"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
SQ   SEQUENCE   239 AA;  26029 MW;  D2EDAD47382A275D CRC64;
     MTLTRKTLFL LTAAFGIHSF QTASADAVVR AEKLHASANR SYKVAGKRYT PKNQVAEFTQ
     TGNASWYGGR FHGRKTSGGE RYDMNAFTAA HKTLPIPSYV RVTNTKNGKS VIVRVNDRGP
     FHGNRIIDVS KAAAQKLGFV NQGTAHVKIE QIVPGQSAPV AENKDIFIDL KSFGTEHEAQ
     AYLNQAAQNL ASSASNPNLS VEKRRYEYVV KMGPFASQER AAEAEAQARG MVRAVLTAG