ID G2FB13_9GAMM Unreviewed; 307 AA.
AC G2FB13;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=ErfK/YbiS/YcfS/YnhG family {ECO:0000313|EMBL:EGW55951.1};
GN ORFNames=TevJSym_aa00950 {ECO:0000313|EMBL:EGW55951.1};
OS endosymbiont of Tevnia jerichonana (vent Tica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=1049564 {ECO:0000313|EMBL:EGW55951.1, ECO:0000313|Proteomes:UP000005167};
RN [1] {ECO:0000313|EMBL:EGW55951.1, ECO:0000313|Proteomes:UP000005167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D.,
RA Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., Hecker M.,
RA Sievert S.M., Schweder T.;
RT "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and Tevnia
RT jerichonana share an identical physiology as revealed by proteogenomic
RT analyses.";
RL ISME J. 0:0-0(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:EGW55951.1}.
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; AFZB01000001; EGW55951.1; -; Genomic_DNA.
DR RefSeq; WP_006473571.1; NZ_AFZB01000001.1.
DR AlphaFoldDB; G2FB13; -.
DR PATRIC; fig|1049564.3.peg.92; -.
DR eggNOG; COG1376; Bacteria.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000005167; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000005167};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..307
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003428716"
FT DOMAIN 96..228
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 307 AA; 34722 MW; B3719D0FFD807AF1 CRC64;
MRLPYFILFC LGLSWLQTSA ALTFSLPPEG EDLVGELIEL KTRYEDTFSD IARGHDMGFR
EVSQANPGVD AWLPGEGTEI FVPQLFILPD VPREGVVINL AELRLYYYPK DQAQVITYPL
GIGREGWGTP EGATHVIRKR AHPSWYVPES IRQEHQKMGD PLPEVMPPGP DNPLGEYAIY
LGMRGYLLHG TNKPYGVGMR VSHGCIRLYP EDIEEFFRQI PVNTPVRIIN RPYKAGWRDG
QLYVEAHPPL NEQIKVEGRN HTGLVTAMIT KLGEDRRQPD WDILQTIARD QTGIPEIVPL
SELPGDN
//
