ID   RLPA_PASMU              Reviewed;         294 AA.
AC   Q9CJR6;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 113.
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=PM1926;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK04010.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9CJR6; -.
DR   SMR; Q9CJR6; -.
DR   STRING; 747.DR93_8; -.
DR   EnsemblBacteria; AAK04010; AAK04010; PM1926.
DR   KEGG; pmu:PM1926; -.
DR   HOGENOM; CLU_042923_3_1_6; -.
DR   OMA; HKFNGRK; -.
DR   Proteomes; UP000000809; 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   Gene3D; 3.30.70.1070; -; 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   Pfam; PF03330; DPBB_1; 1.
DR   Pfam; PF05036; SPOR; 1.
DR   SUPFAM; SSF110997; SSF110997; 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..23
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT   CHAIN           24..294
FT                   /note="Endolytic peptidoglycan transglycosylase RlpA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT                   /id="PRO_0000030808"
FT   DOMAIN          216..291
FT                   /note="SPOR"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
SQ   SEQUENCE   294 AA;  33049 MW;  403FE0749D1667B5 CRC64;
     MKQKIFQILT ALCCIFYVMS AQAIDAKKLY GLQGPKLIYQ APVTKSHHYV VKGVSYRTQT
     SKEASGYARD GIASFYHKKF NGRKTASGQI YNENLYTAAH KTLPLNSYVL VTNLRNQRKV
     IVRINDRGPF VKGRIIDLSR AAAREIGLIG SGVGHVRVEL IQLDRQGRIS GAASATLAKL
     AKNQEAVNML LQGEDTVELT QHTEEKTVKA ATTKPEKYTT VYKIRILNLD SKKQAEKLIS
     KLGREDIRAD ITVNQDKFDI YFGPFSDKSQ VNDVKAQLRK LNYSKPLIVY TFDD