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Database: UniProt
Entry: A0A0B4EIC9_9RHOB
LinkDB: A0A0B4EIC9_9RHOB
Original site: A0A0B4EIC9_9RHOB 
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
//
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