ID   A0A136JL49_9BACT        Unreviewed;       314 AA.
AC   A0A136JL49;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=YkuD domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=UZ19_OD1000921 {ECO:0000313|EMBL:KXJ97857.1};
OS   Parcubacteria bacterium OLB19.
OC   Bacteria; Candidatus Parcubacteria.
OX   NCBI_TaxID=1617425 {ECO:0000313|EMBL:KXJ97857.1, ECO:0000313|Proteomes:UP000070365};
RN   [1] {ECO:0000313|EMBL:KXJ97857.1, ECO:0000313|Proteomes:UP000070365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB19 {ECO:0000313|EMBL:KXJ97857.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Improved understanding of the partial-nitritation anammox process through
RT   23 genomes representing the majority of the microbial community.";
RL   Submitted (MAR-2015) 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:KXJ97857.1}.
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DR   EMBL; JZEL01000029; KXJ97857.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136JL49; -.
DR   STRING; 1617425.UZ19_OD1000921; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000070365; 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; 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   PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30582:SF2; SLL0670 PROTEIN; 1.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        9..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          108..170
FT                   /note="SH3b"
FT                   /evidence="ECO:0000259|Pfam:PF08239"
FT   DOMAIN          191..312
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
SQ   SEQUENCE   314 AA;  35946 MW;  486912704022A38E CRC64;
     MKKKTKKNIW YITLVVVEAL CIIALSFMIF VLLQDGFDNY GTNENQSPQT AEEQKTDFLT
     DEEGVMIIEN PDKGTESPEE VIIPINRVLF EYIEVFDSCG PHFEGECLNA RSGPGTDYPA
     TAKLRKGVVL KVDGEVERDN GEIWYKVVFD EWLRYPERVK GDWYVNSDYV EVLLDEGDKT
     IWDHGKATST KEIIVDRSEQ KLYAYENDEL FMEISISTGL ELTPTPRGTF TVFKKTPSRY
     MQGPLPNLID QQYYDLPGVP WNLYFTDGGA VIHGAYWHNS FGRKYSHGCV NVPIDKAREL
     YSWTPLGTKV TVKD
//