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Database: UniProt
Entry: A0A099FA82_9RHOB
LinkDB: A0A099FA82_9RHOB
Original site: A0A099FA82_9RHOB 
ID   A0A099FA82_9RHOB        Unreviewed;       171 AA.
AC   A0A099FA82;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=ErfK/YbiS/YcfS/YnhG family protein {ECO:0000313|EMBL:KGJ07163.1};
GN   ORFNames=IC63_09430 {ECO:0000313|EMBL:KGJ07163.1};
OS   Paracoccus sphaerophysae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=690417 {ECO:0000313|EMBL:KGJ07163.1, ECO:0000313|Proteomes:UP000029917};
RN   [1] {ECO:0000313|EMBL:KGJ07163.1, ECO:0000313|Proteomes:UP000029917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAMBI 3106 {ECO:0000313|EMBL:KGJ07163.1,
RC   ECO:0000313|Proteomes:UP000029917};
RA   McGinnis J.M., Wolfgang W.J.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KGJ07163.1, ECO:0000313|Proteomes:UP000029917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAMBI 3106 {ECO:0000313|EMBL:KGJ07163.1,
RC   ECO:0000313|Proteomes:UP000029917};
RA   Mingle L.A., Cole J.A., Lapierre P., Musser K.A.;
RT   "Paracoccus sanguinis sp. nov., isolated from clinical specimens of New
RT   York State patients.";
RL   Submitted (OCT-2014) 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}.
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:KGJ07163.1}.
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DR   EMBL; JRKS01000025; KGJ07163.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A099FA82; -.
DR   STRING; 690417.IC63_09430; -.
DR   OrthoDB; 9809748at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000029917; Unassembled WGS sequence.
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; PTHR36699:SF1; L,D-TRANSPEPTIDASE YAFK-RELATED; 1.
DR   PANTHER; PTHR36699; LD-TRANSPEPTIDASE; 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   Reference proteome {ECO:0000313|Proteomes:UP000029917};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          37..169
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
SQ   SEQUENCE   171 AA;  19381 MW;  26A61452DB343DA3 CRC64;
     MLRPNRRHFS LTMLAALAAC GTQPPVLKRY LGPPVTQVVV QKERRRMYLL SGQTVLKSYD
     FGLGNEPIGH KQFEGDGKTP EGLYYIDRFN PRSRYHLSVG ISYPNERDRA FAEQFGLDPG
     GDIMIHGRGP EGKRLVRQKR DWTAGCITVS DDEVEDIFAM LRLGVPVMIY P
//
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