ID F0RSM8_SPHGB Unreviewed; 220 AA.
AC F0RSM8;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
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};
DE Flags: Precursor;
GN Name=rlpA {ECO:0000256|HAMAP-Rule:MF_02071};
GN OrderedLocusNames=SpiBuddy_2326 {ECO:0000313|EMBL:ADY14144.1};
OS Sphaerochaeta globosa (strain ATCC BAA-1886 / DSM 22777 / Buddy)
OS (Spirochaeta sp. (strain Buddy)).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Sphaerochaetaceae;
OC Sphaerochaeta.
OX NCBI_TaxID=158189 {ECO:0000313|EMBL:ADY14144.1, ECO:0000313|Proteomes:UP000008466};
RN [1] {ECO:0000313|Proteomes:UP000008466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1886 / DSM 22777 / Buddy
RC {ECO:0000313|Proteomes:UP000008466};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Zeytun A., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Mikhailova N., Pagani I., Ritalahti K.M., Loeffler F.E.,
RA Woyke T.;
RT "Complete sequence of Spirochaeta sp. Buddy.";
RL Submitted (FEB-2011) 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; CP002541; ADY14144.1; -; Genomic_DNA.
DR RefSeq; WP_013607993.1; NC_015152.1.
DR AlphaFoldDB; F0RSM8; -.
DR STRING; 158189.SpiBuddy_2326; -.
DR KEGG; sbu:SpiBuddy_2326; -.
DR eggNOG; COG0797; Bacteria.
DR HOGENOM; CLU_042923_3_4_12; -.
DR OrthoDB; 9779128at2; -.
DR Proteomes; UP000008466; 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; 2.40.40.10; RlpA-like domain; 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 NCBIfam; TIGR00413; rlpA; 1.
DR PANTHER; PTHR34183; -; 1.
DR PANTHER; PTHR34183:SF1; ENDOLYTIC PEPTIDOGLYCAN TRANSGLYCOSYLASE RLPA; 1.
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 Lipoprotein {ECO:0000313|EMBL:ADY14144.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02071};
KW Reference proteome {ECO:0000313|Proteomes:UP000008466};
KW Signal {ECO:0000256|HAMAP-Rule:MF_02071}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02071"
FT CHAIN 21..220
FT /note="Probable endolytic peptidoglycan transglycosylase
FT RlpA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02071"
FT /id="PRO_5009991432"
FT DOMAIN 32..120
FT /note="RlpA-like protein double-psi beta-barrel"
FT /evidence="ECO:0000259|Pfam:PF03330"
SQ SEQUENCE 220 AA; 24254 MW; A72720EB15C8CA26 CRC64;
MKRLMALLAV LLLSSLWLFA ADEPLQPGSV IEKGIASWYT TDKSESLTAN GEIFDPNVLS
AAHKSLKFGT IVRVTNLANG KSVDVRINDR GPYVDGRIID LTPAAAKQID MLNSGISSVD
LTLIFEPEVP ESKYNRAGDT GWYQIQVGAY SSLLTAYAQY DRLLNAGLKP YAEQLPDSQA
VRLTVRWVPA YQLDRTMKAL SALGFAEKNV LKKSEVNPYR
//
