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Database: UniProt
Entry: F4D1T8_PSEUX
LinkDB: F4D1T8_PSEUX
Original site: F4D1T8_PSEUX 
ID   F4D1T8_PSEUX            Unreviewed;       407 AA.
AC   F4D1T8;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=ErfK/YbiS/YcfS/YnhG family protein {ECO:0000313|EMBL:AEA27998.1};
GN   OrderedLocusNames=Psed_5874 {ECO:0000313|EMBL:AEA27998.1};
OS   Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 /
OS   CB1190).
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=675635 {ECO:0000313|EMBL:AEA27998.1, ECO:0000313|Proteomes:UP000007809};
RN   [1] {ECO:0000313|EMBL:AEA27998.1, ECO:0000313|Proteomes:UP000007809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190
RC   {ECO:0000313|Proteomes:UP000007809};
RX   PubMed=21725009; DOI=10.1128/JB.00415-11;
RA   Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A., Woyke T.,
RA   Nolan M., Lapidus A., Chertkov O., Ovchinnikova G., Sczyrba A.,
RA   Alvarez-Cohen L.;
RT   "Genome sequence of the 1,4-dioxane-degrading Pseudonocardia dioxanivorans
RT   strain CB1190.";
RL   J. Bacteriol. 193:4549-4550(2011).
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
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DR   EMBL; CP002593; AEA27998.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4D1T8; -.
DR   STRING; 675635.Psed_5874; -.
DR   KEGG; pdx:Psed_5874; -.
DR   eggNOG; COG1376; Bacteria.
DR   HOGENOM; CLU_039404_3_0_11; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000007809; Chromosome.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd13432; LDT_IgD_like_2; 1.
DR   CDD; cd16913; YkuD_like; 1.
DR   Gene3D; 2.60.40.3710; -; 1.
DR   Gene3D; 2.60.40.3780; -; 1.
DR   Gene3D; 2.40.440.10; L,D-transpeptidase catalytic domain-like; 1.
DR   InterPro; IPR041280; Big_10.
DR   InterPro; IPR005490; LD_TPept_cat_dom.
DR   InterPro; IPR038063; Transpep_catalytic_dom.
DR   PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30582:SF35; L,D-TRANSPEPTIDASE 2; 1.
DR   Pfam; PF17964; Big_10; 1.
DR   Pfam; PF03734; YkuD; 1.
DR   SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007809};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          70..231
FT                   /note="Bacterial Ig"
FT                   /evidence="ECO:0000259|Pfam:PF17964"
FT   DOMAIN          257..376
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
SQ   SEQUENCE   407 AA;  42223 MW;  6CF6736C0B337329 CRC64;
     MRGPTGRVRT RLSFSLGVAV LACLVLAGLV IAAPRQAQAL SAGITSGAGG QPAAAAAPVV
     ATSADSGPLN PSSPLQLTVT GGTIAAVAMT DKADGKPVAG TLAPGGAGWA STGDLAYGTT
     YSVGVDTVAA DGTRHHDDKT VSTVAPRTTA YPSFIPPPSQ TSVGVGQPIV VRFDHAVHDK
     ATAEKALSVT ASPPQEGSWY WLSATEAHYR PKTYWQAGST ITLKADMFGV DLGDGTYGET
     DRTETIHVHD SWIAKADGAT EQMQIFQNGK LVNTMPISLG SPGFPSHTGP HVISDKQPSI
     IMDSCTYGVC QGQPGYYKEQ VDLDERISDD GEFVHSAPWS VGSQGGANVS HGCVNLSPAN
     AQWFFDHFGI GDVVEITNSG GPTLPLGDTY GDWELSWSQW QAGSAAK
//
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