ID   A0A410DMS1_9CLOT        Unreviewed;       450 AA.
AC   A0A410DMS1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=L,D-transpeptidase catalytic domain-containing protein {ECO:0000259|Pfam:PF03734};
GN   ORFNames=C1I91_01045 {ECO:0000313|EMBL:QAA30380.1};
OS   Clostridium manihotivorum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=2320868 {ECO:0000313|EMBL:QAA30380.1, ECO:0000313|Proteomes:UP000286268};
RN   [1] {ECO:0000313|EMBL:QAA30380.1, ECO:0000313|Proteomes:UP000286268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT4 {ECO:0000313|EMBL:QAA30380.1,
RC   ECO:0000313|Proteomes:UP000286268};
RA   Tachaapaikoon C., Sutheeworapong S., Jenjaroenpun P., Wongsurawat T.,
RA   Nookeaw I., Cheawchanlertfa P., Kosugi A., Cheevadhanarak S.,
RA   Ratanakhanokchai K.;
RT   "Genome Sequencing and Assembly of Anaerobacter polyendosporus strain
RT   CT4.";
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP025746; QAA30380.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A410DMS1; -.
DR   KEGG; cmah:C1I91_01045; -.
DR   OrthoDB; 177750at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000286268; Chromosome.
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; 2.40.440.10; L,D-transpeptidase catalytic domain-like; 1.
DR   InterPro; IPR005490; LD_TPept_cat_dom.
DR   InterPro; IPR038063; Transpep_catalytic_dom.
DR   PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR   Pfam; PF03734; YkuD; 1.
DR   SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286268};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          328..449
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
FT   REGION          243..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..305
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   450 AA;  50520 MW;  1BF3839828940DE2 CRC64;
     MENDKNDIID ESNEVNESIK KRKPPLSKII ILSIFALFCI AMSYSFYAYN DIISDFKIDF
     DKKDYSAANS LIVSKGNFNP AKKLLLYGDL KNYFSTYIDD LISNYKNNNI SDETALSVLN
     EVDRYGVVSD KIREFKKKIP LLTDSANNFS LGMKLYKDKN YADAYAAFDK VNNYDDNFLK
     AEEYKKEVAN CIKQETLSSA EKLVSENYFS KAISLLEDNT KYYSNDKEVL SKIDEYKKDK
     DDFVNKSSSS KTSANDKDDS ASNSTSSNTA TTNSSKDSKT DSPKSSSKSE NGTNKSSTDS
     SSKTTSVSAM VINSNTINSL NLSSDTSYLV YVNLSSQKTY VYKGKKNGWN LLKGFSCSTG
     IKGSETPSGI FTVKEKGDWF YSDEYKEGAK YWVQFDGNYL FHSLPYNSSK SQITDFTLGK
     AASHGCVRLK VEDAKWIYDN VSRGSKVIIN
//