ID Q20X92_RHOPB Unreviewed; 265 AA.
AC Q20X92;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=ErfK/YbiS/YcfS/YnhG {ECO:0000313|EMBL:ABD90244.1};
GN OrderedLocusNames=RPC_4722 {ECO:0000313|EMBL:ABD90244.1};
OS Rhodopseudomonas palustris (strain BisB18).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316056 {ECO:0000313|EMBL:ABD90244.1};
RN [1] {ECO:0000313|EMBL:ABD90244.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB18 {ECO:0000313|EMBL:ABD90244.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SIMILARITY: Belongs to the YkuD family.
CC {ECO:0000256|ARBA:ARBA00005992}.
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DR EMBL; CP000301; ABD90244.1; -; Genomic_DNA.
DR AlphaFoldDB; Q20X92; -.
DR STRING; 316056.RPC_4722; -.
DR MEROPS; C82.003; -.
DR KEGG; rpc:RPC_4722; -.
DR eggNOG; COG1376; Bacteria.
DR HOGENOM; CLU_042399_1_0_5; -.
DR OrthoDB; 9813664at2; -.
DR UniPathway; UPA00219; -.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProt.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd16913; YkuD_like; 1.
DR Gene3D; 2.40.440.10; L,D-transpeptidase catalytic domain-like; 1.
DR InterPro; IPR005490; LD_TPept_cat_dom.
DR InterPro; IPR038063; Transpep_catalytic_dom.
DR PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30582:SF24; L,D-TRANSPEPTIDASE ERFK_SRFK-RELATED; 1.
DR Pfam; PF03734; YkuD; 1.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..265
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004199588"
FT DOMAIN 136..264
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 265 AA; 28961 MW; FCBDCCDE667B8C6E CRC64;
MLKKATLALL TGASCLGAGL SPAAAIEIEM PGAPSVIYAD EPPPPMRMAS SQRPRMGGGF
IEFLFSDGPA QPGYGEPAPR YQVPPDDYEP RQRMLLPAEP QQSLRPDEQA VDPQQQPFDP
KYEKQLVAYH GKETPGTIVI DTPNKFLFLV QGDGTALRYG IGVGRPGFTW SGVKQISAKK
EWPAWTPPPE MLARRPDLPR HMEGGPQNPL GARAMYLGST LYRIHGSNEP WTIGTNVSSG
CIRMRNEDVI DLYGRVNVGA RVIVI
//
