ID A0A411YHU6_9ACTN Unreviewed; 625 AA.
AC A0A411YHU6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
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 ORFNames=ER308_14710 {ECO:0000313|EMBL:QBI20686.1};
OS Egibacter rhizosphaerae.
OC Bacteria; Actinomycetota; Nitriliruptoria; Egibacterales; Egibacteraceae;
OC Egibacter.
OX NCBI_TaxID=1670831 {ECO:0000313|EMBL:QBI20686.1, ECO:0000313|Proteomes:UP000291469};
RN [1] {ECO:0000313|EMBL:QBI20686.1, ECO:0000313|Proteomes:UP000291469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EGI 80759 {ECO:0000313|EMBL:QBI20686.1,
RC ECO:0000313|Proteomes:UP000291469};
RA Chen D.-D., Tian Y., Jiao J.-Y., Zhang X.-T., Zhang Y.-G., Zhang Y.,
RA Xiao M., Shu W.-S., Li W.-J.;
RT "Egibacter rhizosphaerae EGI 80759T.";
RL Submitted (JAN-2019) 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 -!- SIMILARITY: Belongs to the RlpA family. {ECO:0000256|HAMAP-
CC Rule:MF_02071, ECO:0000256|RuleBase:RU003495}.
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DR EMBL; CP036402; QBI20686.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411YHU6; -.
DR KEGG; erz:ER308_14710; -.
DR OrthoDB; 9813435at2; -.
DR Proteomes; UP000291469; Chromosome.
DR GO; GO:0008932; F:lytic endotransglycosylase activity; IEA:UniProtKB-UniRule.
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; 3.40.50.12090; -; 1.
DR Gene3D; 2.40.40.10; RlpA-like domain; 1.
DR HAMAP; MF_02071; RlpA; 1.
DR InterPro; IPR007253; Cell_wall-bd_2.
DR InterPro; IPR034718; RlpA.
DR InterPro; IPR009009; RlpA-like_DPBB.
DR InterPro; IPR036908; RlpA-like_sf.
DR InterPro; IPR012997; RplA.
DR NCBIfam; TIGR00413; rlpA; 1.
DR PANTHER; PTHR34183; -; 1.
DR PANTHER; PTHR34183:SF1; ENDOLYTIC PEPTIDOGLYCAN TRANSGLYCOSYLASE RLPA; 1.
DR Pfam; PF04122; CW_binding_2; 2.
DR Pfam; PF03330; DPBB_1; 1.
DR SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_02071};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02071};
KW Reference proteome {ECO:0000313|Proteomes:UP000291469}.
FT DOMAIN 528..618
FT /note="RlpA-like protein double-psi beta-barrel"
FT /evidence="ECO:0000259|Pfam:PF03330"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..143
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..522
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 625 AA; 64636 MW; 96E632F718024129 CRC64;
MRCGPASRGR RPTCAASTRT RAPRTVAESG RTVASPGPVV RRPTPVGARR APVAHCGGRS
PTRGRVAVAQ GEVSGGTSGA IAATGSLGTI RVPSAGRVPS SRSTHRAGRT RRVRGHEGSL
PRRDAAPPTT TPDPTPDPHT PPHKASPMTL SRTQLLRRVT TRAAVIAAGA LMVPVAATPV
LADDEDEVVR LAAGNDRIET AIETSKAAGD DAREALLVHE DGYPDALAAG SVAGELDAPL
LYTDGAGLDP RVADELDRLG TERVWVFGGP AAIDETVTDA LADADLEVER IDGDTRVGTA
AAAATELHDE IDTATLALGF SADDRPGWPD AGAAATFAGA GATPTLLSRH DSVPQVTLDA
LDELDVERVQ LIGGQHVLAD GVSDELERAG FDVERHSGET RAATAARVAD RVLDGAAEDA
EFTAVLVDGR AQPDVFLAGG LAARIGGTVL FSGRDQLSSH AEEALRRDRV TGATVVGGGL
HSWVVDSASA AASGDDLPEP PDELVEEEPA EAEEEAEPEG PEVVDVVEGE ASWYGDRFAG
RPTASGEPYD PNALTAAMPP GTVAFGTWVR VTYLATDRSV EVRINDRGPY AGNRVIDLSR
AAADTIGLRS AGTGQVRIEV LDGAP
//