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Database: UniProt
Entry: Q8G821_BIFLO
LinkDB: Q8G821_BIFLO
Original site: Q8G821_BIFLO 
ID   Q8G821_BIFLO            Unreviewed;       180 AA.
AC   Q8G821;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   SubName: Full=Protein similar to YcbI of B. subtilis {ECO:0000313|EMBL:AAN23928.1};
GN   OrderedLocusNames=BL0062 {ECO:0000313|EMBL:AAN23928.1};
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=206672 {ECO:0000313|EMBL:AAN23928.1, ECO:0000313|Proteomes:UP000000439};
RN   [1] {ECO:0000313|EMBL:AAN23928.1, ECO:0000313|Proteomes:UP000000439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705 {ECO:0000313|Proteomes:UP000000439};
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
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DR   EMBL; AE014295; AAN23928.1; -; Genomic_DNA.
DR   RefSeq; NP_695292.1; NC_004307.2.
DR   RefSeq; WP_011067943.1; NC_004307.2.
DR   AlphaFoldDB; Q8G821; -.
DR   EnsemblBacteria; AAN23928; AAN23928; BL0062.
DR   KEGG; blo:BL0062; -.
DR   PATRIC; fig|206672.9.peg.68; -.
DR   HOGENOM; CLU_089260_0_0_11; -.
DR   OrthoDB; 5242394at2; -.
DR   PhylomeDB; Q8G821; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000439; Chromosome.
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:SF34; L,D-TRANSPEPTIDASE YCIB-RELATED; 1.
DR   Pfam; PF03734; YkuD; 1.
DR   SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000439};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          62..179
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   180 AA;  19701 MW;  A3AE1950E9EC0A5F CRC64;
     MSQSAQQSAS RVSASASSLG RQQVPVFNQA IQEQRDKEAQ RARWTNPTGK QPDLSQYSDL
     SVKVSIAKQE VYVQSGGETI YTMIASTGLN DTTPRGNYVI GMRGDHFYNP AEGMGADYWV
     RFNGPFLFHS VPTGANSGEY MEEEGNKLGQ PASHGCVRLT VADAEWFYNQ IPEGTPVTIA
//
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