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
//