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Database: UniProt
Entry: G4E1E7_9GAMM
LinkDB: G4E1E7_9GAMM
Original site: G4E1E7_9GAMM 
ID   G4E1E7_9GAMM            Unreviewed;       222 AA.
AC   G4E1E7;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=ErfK/YbiS/YcfS/YnhG family protein {ECO:0000313|EMBL:EGZ50667.1};
GN   ORFNames=ThisiDRAFT_0126 {ECO:0000313|EMBL:EGZ50667.1};
OS   Thiorhodospira sibirica ATCC 700588.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thiorhodospira.
OX   NCBI_TaxID=765914 {ECO:0000313|EMBL:EGZ50667.1};
RN   [1] {ECO:0000313|EMBL:EGZ50667.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700588 {ECO:0000313|EMBL:EGZ50667.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J.,
RA   Frigaard N.-U., Bryant D., Woyke T.;
RT   "The draft genome of Thiorhodospira sibirica ATCC 700588.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
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:EGZ50667.1}.
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DR   EMBL; AGFD01000002; EGZ50667.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4E1E7; -.
DR   STRING; 765914.ThisiDRAFT_0126; -.
DR   PATRIC; fig|765914.3.peg.134; -.
DR   eggNOG; COG1376; Bacteria.
DR   UniPathway; UPA00219; -.
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   PANTHER; PTHR30582:SF24; L,D-TRANSPEPTIDASE ERFK_SRFK-RELATED; 1.
DR   Pfam; PF03734; YkuD; 1.
DR   SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          65..221
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
SQ   SEQUENCE   222 AA;  25353 MW;  D59A037108EA7771 CRC64;
     MLFPITCALA QSQRWGIWPD LFFDEYLSDE HMVIDDTERA QMQAWREQLK AVLAQHFPQE
     PLSPLVVVRI EEQRLYLFPT AEDEELRIFP ISTSRHGIGS EEGSYKTPQG VHRIRQKIGA
     GQPKGAIFRA RIPTGEIARL VTEPERTPRD NITSRILWLE GLEEGVNRGP GIDSFARYIY
     IHGTDEEGLI GTPASDGCVR MRNQDVIWLY EQLPQGTLVI IQ
//
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