ID Q89UE9_BRADU Unreviewed; 272 AA.
AC Q89UE9;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Blr1468 protein {ECO:0000313|EMBL:BAC46733.1};
GN OrderedLocusNames=blr1468 {ECO:0000313|EMBL:BAC46733.1};
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=224911 {ECO:0000313|EMBL:BAC46733.1, ECO:0000313|Proteomes:UP000002526};
RN [1] {ECO:0000313|Proteomes:UP000002526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110
RC {ECO:0000313|Proteomes:UP000002526};
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SIMILARITY: Belongs to the YkuD family.
CC {ECO:0000256|ARBA:ARBA00005992}.
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DR EMBL; BA000040; BAC46733.1; -; Genomic_DNA.
DR RefSeq; NP_768108.1; NC_004463.1.
DR AlphaFoldDB; Q89UE9; -.
DR STRING; 224911.AAV28_04290; -.
DR MEROPS; C82.003; -.
DR EnsemblBacteria; BAC46733; BAC46733; BAC46733.
DR KEGG; bja:blr1468; -.
DR PATRIC; fig|224911.5.peg.1528; -.
DR eggNOG; COG1376; Bacteria.
DR HOGENOM; CLU_042399_0_2_5; -.
DR InParanoid; Q89UE9; -.
DR OrthoDB; 9813664at2; -.
DR PhylomeDB; Q89UE9; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0071972; F:peptidoglycan L,D-transpeptidase activity; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0018104; P:peptidoglycan-protein cross-linking; IBA:GO_Central.
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:UP000002526};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..39
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 40..272
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004304822"
FT DOMAIN 102..229
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 58..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 272 AA; 29444 MW; 47EA3589C9939005 CRC64;
MGQHMTKVSL VRRSFSPRAA AAFAFATALL AVPFGSANAQ TLGYAPMQPQ AYLPQPQAYQ
QDPSYSQGYV SEPAQTADED AQLPDRLRKQ VVSFDRSEPA GTIVIDTGNT YLYYVLGNGR
AIRYGVGVGR EGFTWSGVQS VSRKAEWPDW HPPAEMIARQ PYLPRFVAGG PGNPLGARAM
YLGSSEYRIH GTNDPTTIGK FVSSGCIRMT NEDVTDLFSR VNIGARVVVL PKNAPLMAKG
SDRGSDSWRK RPAATTLPSG RQALNISTSA VN
//
