ID A0A0B4EIC9_9RHOB Unreviewed; 200 AA.
AC A0A0B4EIC9;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=ErfK/YbiS/YcfS/YnhG protein {ECO:0000313|EMBL:KID10593.1};
GN ORFNames=GC1_02595 {ECO:0000313|EMBL:KID10593.1};
OS Leisingera sp. ANG1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Leisingera.
OX NCBI_TaxID=1002340 {ECO:0000313|EMBL:KID10593.1, ECO:0000313|Proteomes:UP000031201};
RN [1] {ECO:0000313|EMBL:KID10593.1, ECO:0000313|Proteomes:UP000031201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG1 {ECO:0000313|EMBL:KID10593.1,
RC ECO:0000313|Proteomes:UP000031201};
RX PubMed=21551313; DOI=10.1128/JB.05139-11;
RA Collins A.J., Nyholm S.V.;
RT "Draft genome of Phaeobacter gallaeciensis ANG1, a dominant member of the
RT accessory nidamental gland of Euprymna scolopes.";
RL J. Bacteriol. 193:3397-3398(2011).
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:KID10593.1}.
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DR EMBL; AFCF02000001; KID10593.1; -; Genomic_DNA.
DR RefSeq; WP_019296913.1; NZ_AFCF02000001.1.
DR AlphaFoldDB; A0A0B4EIC9; -.
DR STRING; 1002340.GC1_02595; -.
DR eggNOG; COG1376; Bacteria.
DR OrthoDB; 9795305at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000031201; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProt.
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 3: Inferred from homology;
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 71..198
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 113..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 200 AA; 22385 MW; B134017C77F11087 CRC64;
MTKLRITRRA TLMGLGATLA TPALLRAQST DAFPQNEPAI REEVPVQRNT SAFTQQNWQD
HFETLGVGCL LADISSRALH YWGADGETYR LFPSSVPMTE DLTKRGYTEV VRKKENPSWT
PTASMRERDP SLPVTIEGGV PNNPLGTRAM YLDWPAYLVH GTHDTRKIGR QSSSGCIGLY
NQHVEDLYEL VQIGTQVRLL
//