ID A0A0J1G683_9FIRM Unreviewed; 720 AA.
AC A0A0J1G683;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=YkuD domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=RHS_3066 {ECO:0000313|EMBL:KLU71152.1};
OS Robinsoniella sp. RHS.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Robinsoniella.
OX NCBI_TaxID=1504536 {ECO:0000313|EMBL:KLU71152.1, ECO:0000313|Proteomes:UP000036477};
RN [1] {ECO:0000313|EMBL:KLU71152.1, ECO:0000313|Proteomes:UP000036477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHS {ECO:0000313|EMBL:KLU71152.1};
RX PubMed=25284151; DOI=10.1016/j.cell.2014.09.008;
RA Seedorf H., Griffin N.W., Ridaura V.K., Reyes A., Cheng J., Rey F.E.,
RA Smith M.I., Simon G.M., Scheffrahn R.H., Woebken D., Spormann A.M.,
RA Van Treuren W., Ursell L.K., Pirrung M., Robbins-Pianka A., Cantarel B.L.,
RA Lombard V., Henrissat B., Knight R., Gordon J.I.;
RT "Bacteria from diverse habitats colonize and compete in the mouse gut.";
RL Cell 159:253-266(2014).
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:KLU71152.1}.
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DR EMBL; JNGB01000029; KLU71152.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J1G683; -.
DR PATRIC; fig|1504536.3.peg.3675; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000036477; 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; 2.
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:UP000036477};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 263..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 334..444
FT /note="YoaR-like putative peptidoglycan binding"
FT /evidence="ECO:0000259|Pfam:PF12229"
FT DOMAIN 461..566
FT /note="YoaR-like putative peptidoglycan binding"
FT /evidence="ECO:0000259|Pfam:PF12229"
FT DOMAIN 594..716
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 1..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 720 AA; 82351 MW; 9536594A32CD165A CRC64;
MKMKEEKREE LENEKVTGVG KDAENHINKE SQDKTPDVQE NSADISDKEK QEENAEEKQE
ENVNGQVKEK QDINVEEKQE IKQNEEVVQE VKYEVEHEEK GDTENKAKDE AKDEAKDEAK
DEVKDDVKDD VKDDVKDEVK DDEKDDVKDD VKDDEKDDVK DKAKDKAKDD VKDEAKDEAK
DEVNQEVKQE QKDQLNGELK EEQKDQPNGE SLEKLKETQD PERNEETGNA EAHSTIESNE
HDPIEESEDA SRQGKKGRLW KKLLIGFGCF LLLCVLGVYI GGAVYFQDKF FFNTKVNGID
VSKQTVEMVD NSIANKIHKY TITLSERGKV KEKITADQIG YHYVSKGEVQ GFKDQQNPYT
WPRALWENYR YKFDSSTTYD EKKLAKTLKS LECMNEKNIV APKDAFMKFG ETTYEIEPEV
EGNKVDYDKM VSLVKNLIEH GEKKASLEKN DCYVQPAVRS DNEHLNMLMN NLNQYCRTSI
TFAFGEKREV LDGKTIKDWV SHDEAGTVTF DEEQVRNYVA MLADKYDTYD RPREFKTNDG
SMVTVKGGSY GWMIDQEQEI VDLTKLIQLG AVQERTPAFA RTAVSFDNSD LGQDYVEIDL
TRQHLWMYIG GQVAVSSDFV SGSMVKAGCA TPGGTYTLYY KKSPDVLRSD KPGDSYATPV
TYWMPFNGGI GLHDANWRGS FGGNIYQYNG SHGCINLPTD AARQIYEQIY KGFPIICYYR
//
