GenomeNet

Database: UniProt
Entry: A0A370GGC5_9COXI
LinkDB: A0A370GGC5_9COXI
Original site: A0A370GGC5_9COXI 
ID   A0A370GGC5_9COXI        Unreviewed;       290 AA.
AC   A0A370GGC5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=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   ORFNames=C8D86_11246 {ECO:0000313|EMBL:RDI42848.1};
OS   Aquicella lusitana.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Aquicella.
OX   NCBI_TaxID=254246 {ECO:0000313|EMBL:RDI42848.1, ECO:0000313|Proteomes:UP000254720};
RN   [1] {ECO:0000313|EMBL:RDI42848.1, ECO:0000313|Proteomes:UP000254720}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16500 {ECO:0000313|EMBL:RDI42848.1,
RC   ECO:0000313|Proteomes:UP000254720};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (JUL-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RDI42848.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; QQAX01000012; RDI42848.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A370GGC5; -.
DR   Proteomes; UP000254720; Unassembled WGS sequence.
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:UP000254720};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..290
FT                   /note="Endolytic peptidoglycan transglycosylase RlpA"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017093072"
FT   DOMAIN          211..290
FT                   /note="SPOR"
FT                   /evidence="ECO:0000259|PROSITE:PS51724"
SQ   SEQUENCE   290 AA;  32630 MW;  A8CE28924109C566 CRC64;
     MSRHPRGALL VLFLMLLLSS CSHVGKKDGP PNFYVDETKI PNAVPKPEPR AKYGNMTSYR
     VFGKRYYTLK SSKNYEAVGT ASWYGTLFHD RRTSSGEPYD MLGMTAAHKT LPLPTYVEVT
     NLKNKRKIIV KVNDRGPFEG NRLIDLSYVA AKKLGMLGHG TALVKVKAIN PRTYERDQFF
     VASRQAKHKK QFAENNKRDF LLTEDPLLPE NKSAQSVYLQ VGAFRNKSRA EKLKQRLIAL
     LEAPVKISSP SASGKFYRVK VGPIKDVAME DKITHRLKGM GIKPNKTNDG
//
DBGET integrated database retrieval system