ID   A0A1G6AYM7_9FIRM        Unreviewed;       535 AA.
AC   A0A1G6AYM7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Putative peptidoglycan binding domain-containing protein {ECO:0000313|EMBL:SDB13517.1};
GN   ORFNames=SAMN02910317_00642 {ECO:0000313|EMBL:SDB13517.1};
OS   Ruminococcaceae bacterium FB2012.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae.
OX   NCBI_TaxID=1520817 {ECO:0000313|EMBL:SDB13517.1, ECO:0000313|Proteomes:UP000199364};
RN   [1] {ECO:0000313|EMBL:SDB13517.1, ECO:0000313|Proteomes:UP000199364}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB2012 {ECO:0000313|EMBL:SDB13517.1,
RC   ECO:0000313|Proteomes:UP000199364};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
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DR   EMBL; FMXS01000004; SDB13517.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6AYM7; -.
DR   STRING; 1520817.SAMN02910317_00642; -.
DR   OrthoDB; 3176960at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000199364; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.10.20.800; -; 1.
DR   Gene3D; 2.40.440.10; L,D-transpeptidase catalytic domain-like; 1.
DR   InterPro; IPR038054; LD_TPept-like_central_sf.
DR   InterPro; IPR005490; LD_TPept_cat_dom.
DR   InterPro; IPR038063; Transpep_catalytic_dom.
DR   InterPro; IPR022029; YoaR-like_PG-bd.
DR   PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30582:SF2; SLL0670 PROTEIN; 1.
DR   Pfam; PF12229; PG_binding_4; 1.
DR   Pfam; PF03734; YkuD; 1.
DR   SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR   SUPFAM; SSF143985; L,D-transpeptidase pre-catalytic domain-like; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199364};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        56..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          277..375
FT                   /note="YoaR-like putative peptidoglycan binding"
FT                   /evidence="ECO:0000259|Pfam:PF12229"
FT   DOMAIN          409..532
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   535 AA;  61636 MW;  27E7A179B56467A7 CRC64;
     MSGEQKPRMT NDDLARKIRE NMQRNERAAS RPKRRPQQSG RAPAKVKAKT MSPVKAVVIT
     IIIILVLVLG FLTFLYFRGL RNAQGKFLDN TYINDIEVSE LTESEAYNKV KASITFPQAV
     TLVKPDGTKI EFPLENLGYQ DNVKTTVSQY MSQQNYYLWF THSSGRTDYR FEPEFKYDRS
     LLISEIRRRM LNASGSTEAK DAYIKHTKNG FEVVKEVIGD YIDDKKLDTL VDHVTKELDK
     GSYEIDLVGL DLYQRPKVVA ADLEDDLREL ESIDDMEITI DFIYEKAVLK GSEFKDWIKY
     DEDNALNGFT VDEKKVMAYV EQLAAKYDTY NTVRTFKSTT RGKIKVEQGE GCYGFWLYQD
     KMCQKIISLI KNCDSCEIEP IYYVNPYSNY VYDCDPQYRT EKTDIGNTYC EVDLAAQHFW
     YYEKGKLQYE CDIVSGKDTP ERRTPAGIYK VWLKEKNKLL TGSTSAGESW STPTTYWNNI
     STFGIGLHDA SWRGSYFGGT IYKYDGSHGC INMPVNAAKY VYENVPIGTP VVMYW
//