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Database: UniProt
Entry: D0GIG9_9FUSO
LinkDB: D0GIG9_9FUSO
Original site: D0GIG9_9FUSO 
ID   D0GIG9_9FUSO            Unreviewed;       575 AA.
AC   D0GIG9;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=ErfK/YbiS/YcfS/YnhG {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF0554_0230 {ECO:0000313|EMBL:EEY36115.1};
OS   Pseudoleptotrichia goodfellowii F0264.
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC   Pseudoleptotrichia.
OX   NCBI_TaxID=596323 {ECO:0000313|EMBL:EEY36115.1, ECO:0000313|Proteomes:UP000004226};
RN   [1] {ECO:0000313|EMBL:EEY36115.1, ECO:0000313|Proteomes:UP000004226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0264 {ECO:0000313|EMBL:EEY36115.1,
RC   ECO:0000313|Proteomes:UP000004226};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
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:EEY36115.1}.
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DR   EMBL; ADAD01000010; EEY36115.1; -; Genomic_DNA.
DR   RefSeq; WP_006806274.1; NZ_ADAD01000010.1.
DR   AlphaFoldDB; D0GIG9; -.
DR   eggNOG; COG1376; Bacteria.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000004226; Unassembled WGS sequence.
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   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR005490; LD_TPept_cat_dom.
DR   InterPro; IPR003646; SH3-like_bac-type.
DR   InterPro; IPR038063; Transpep_catalytic_dom.
DR   Pfam; PF08239; SH3_3; 1.
DR   Pfam; PF03734; YkuD; 1.
DR   SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000004226};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..575
FT                   /note="ErfK/YbiS/YcfS/YnhG"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003007914"
FT   DOMAIN          242..297
FT                   /note="SH3b"
FT                   /evidence="ECO:0000259|Pfam:PF08239"
FT   DOMAIN          421..553
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
FT   REGION          125..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..140
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   575 AA;  65200 MW;  E162D50197EF517B CRC64;
     MKLRKLQLLG MIILMSSLMY AAPLGTAPAN TGTLKNWKTV EMTPDLDKDG KKDKLVIEYS
     EQNDKIYTKF TPYVNDDSNK AVKGQTVEKI FERANFQKDF NNFSREFVKN YPKKVKTASK
     PVNTTVTSVQ PNTQNKQPVK NDKPLIPPTQ NVGKEVEDKA AVPQDLKETG KNPKEVIPDE
     QTDKEIQKVD GKPVDKKEEL IKGPYPYVTY YLKERPKNLT FDYKYAKNSP RDMDEFIFIK
     TATNIRKEPN ANAASIKKAS YGHKYKVVGK VKTNAKGGTA EWYEVYFDGK LGYVLNSVAV
     KREFDWQDMM KKVEKTNKFV NEAVSKGQTI YVLDDYVPLG GGSGSSKDKF GNRENQSERG
     YLGADFKEFI NLPDRTMMTI LEETDKYLKV KVDAYDNGTY YLKKSKKSLL KDSKITGEIT
     RFIYVDRHSQ NEMIIEKNTN ANTWNVVTTS FVTTGKDAGN SYATPYGTFL IAYSKPVMQY
     TGSDNKTVVG DANNAVRFSG GGYMHSIPSL FEPKETRKSR KAVTARKIGT FPESHKCIRH
     YDDQIKFIYD WLGNSSPGNK LGRRVPSVPT VMLVK
//
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