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Database: UniProt
Entry: I0IMR6_LEPFC
LinkDB: I0IMR6_LEPFC
Original site: I0IMR6_LEPFC 
ID   I0IMR6_LEPFC            Unreviewed;       227 AA.
AC   I0IMR6;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 49.
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=LFE_0856 {ECO:0000313|EMBL:BAM06565.1};
OS   Leptospirillum ferrooxidans (strain C2-3).
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Leptospirillum.
OX   NCBI_TaxID=1162668 {ECO:0000313|EMBL:BAM06565.1, ECO:0000313|Proteomes:UP000007382};
RN   [1] {ECO:0000313|EMBL:BAM06565.1, ECO:0000313|Proteomes:UP000007382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C2-3 {ECO:0000313|EMBL:BAM06565.1,
RC   ECO:0000313|Proteomes:UP000007382};
RX   PubMed=22815442; DOI=10.1128/JB.00696-12;
RA   Fujimura R., Sato Y., Nishizawa T., Oshima K., Kim S.-W., Hattori M.,
RA   Kamijo T., Ohta H.;
RT   "Complete Genome Sequence of Leptospirillum ferrooxidans Strain C2-3,
RT   Isolated from a Fresh Volcanic Ash Deposit on the Island of Miyake,
RT   Japan.";
RL   J. Bacteriol. 194:4122-4123(2012).
RN   [2] {ECO:0000313|Proteomes:UP000007382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C2-3 {ECO:0000313|Proteomes:UP000007382};
RA   Fujimura R., Sato Y., Nishizawa T., Nanba K., Oshima K., Hattori M.,
RA   Kamijo T., Ohta H.;
RT   "The complete genome sequence of the pioneer microbe on fresh volcanic
RT   deposit, Leptospirillum ferrooxidans strain C2-3.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_02071};
CC       Lipid-anchor {ECO:0000256|HAMAP-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; AP012342; BAM06565.1; -; Genomic_DNA.
DR   RefSeq; WP_014449056.1; NC_017094.1.
DR   AlphaFoldDB; I0IMR6; -.
DR   STRING; 1162668.LFE_0856; -.
DR   GeneID; 78148655; -.
DR   KEGG; lfc:LFE_0856; -.
DR   PATRIC; fig|1162668.3.peg.1000; -.
DR   eggNOG; COG0797; Bacteria.
DR   HOGENOM; CLU_042923_3_4_0; -.
DR   OrthoDB; 9779128at2; -.
DR   Proteomes; UP000007382; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS51724; SPOR; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_02071};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_02071};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|HAMAP-
KW   Rule:MF_02071};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02071};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02071};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|HAMAP-Rule:MF_02071};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007382};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..227
FT                   /note="Probable endolytic peptidoglycan transglycosylase
FT                   RlpA"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009991823"
FT   DOMAIN          150..227
FT                   /note="SPOR"
FT                   /evidence="ECO:0000259|PROSITE:PS51724"
SQ   SEQUENCE   227 AA;  25126 MW;  759B67786337D975 CRC64;
     MKLRFTKSLI ALTVAFVFGG CSSFFDTHAH WGYRSNSSRI GGSSDQTFPQ VGVASWYGPT
     FYGKPTASGD IFRKNELTAA HRTLPLGTRV RVQNLNNNKQ VDVLINDRGP FVEGRIIDLS
     WLAAKKIDML GKGTAPVRIT PLNGAAFAQE IQQASYAIQV GTFTHKKDAI TFMNHLKAYS
     HRRVVTSYYR GGQVYRIRVG LYPTLNLAHA AASKLRKSLG EAFVVKL
//
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