ID A7BAA2_9ACTO Unreviewed; 483 AA.
AC A7BAA2;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=ErfK/YbiS/YcfS/YnhG {ECO:0000313|EMBL:EDN80126.1};
GN ORFNames=ACTODO_00563 {ECO:0000313|EMBL:EDN80126.1};
OS Schaalia odontolytica ATCC 17982.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Schaalia.
OX NCBI_TaxID=411466 {ECO:0000313|EMBL:EDN80126.1, ECO:0000313|Proteomes:UP000003553};
RN [1] {ECO:0000313|EMBL:EDN80126.1, ECO:0000313|Proteomes:UP000003553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17982 {ECO:0000313|EMBL:EDN80126.1,
RC ECO:0000313|Proteomes:UP000003553};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDN80126.1, ECO:0000313|Proteomes:UP000003553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17982 {ECO:0000313|EMBL:EDN80126.1,
RC ECO:0000313|Proteomes:UP000003553};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Actinomyces odontolyticus (ATCC 17982).";
RL Submitted (MAY-2007) 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:EDN80126.1}.
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DR EMBL; AAYI02000004; EDN80126.1; -; Genomic_DNA.
DR RefSeq; WP_003791048.1; NZ_DS264586.1.
DR AlphaFoldDB; A7BAA2; -.
DR eggNOG; COG1376; Bacteria.
DR eggNOG; COG5263; Bacteria.
DR HOGENOM; CLU_038468_0_0_11; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000003553; 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; 2.10.270.10; Cholin Binding; 2.
DR Gene3D; 2.40.440.10; L,D-transpeptidase catalytic domain-like; 1.
DR InterPro; IPR018337; Cell_wall/Cho-bd_repeat.
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; PF01473; Choline_bind_1; 4.
DR Pfam; PF19127; Choline_bind_3; 1.
DR Pfam; PF03734; YkuD; 1.
DR SUPFAM; SSF69360; Cell wall binding repeat; 2.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR PROSITE; PS51170; CW; 4.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..483
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039316240"
FT REPEAT 198..217
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 218..237
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 258..277
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 278..297
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT DOMAIN 364..482
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 45..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 52770 MW; 986E184EA71A9E88 CRC64;
MRNISVRLLR CIDASAATIA CIGLFPLAAT ASGAKDIPSV DASSPFAAAS PDVGSEATDP
SGHEDSSPAA DASGPTSERQ ATSQADAATD SVETPSLDHD SASADTEREP TSPEATSGHW
VRHEAGWRYE LVDGTWMKDG IFDVEGRRYA FDARGYVPVG WYKDPSGAWY ASTENGVRTG
WYHEGGSWYH LGDGGTMTTG WLSSGGSWYY LSAGGQMVTG WSHIDGSWYH FDASGAMNAS
KWVRSGSWYY LGNSGAMATG WFIAGGRWYY AESNGAMTTG WVLSDGSWYH LDSSGALSTG
WLRDGGGSWY YLDSARGGAM ATGWSQVGGT WNYFDRWKGF WVSDRAGFEA DWNYAKSLYS
PTNYLVVVDT NAPHCMTFYW ADGSWQPLTD MPCSVGKPST PTITGTFTIK NRGRSFGHGY
TAYWWTQFSG DYLFHSVLYY EGTYTIMDGT LGGHVSHGCV RLRYEDAKWL HDTIPSGTYV
TIY
//
