ID A6QBH3_SULNB Unreviewed; 211 AA.
AC A6QBH3;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=L,D-transpeptidase catalytic domain-containing protein {ECO:0000259|Pfam:PF03734};
GN OrderedLocusNames=SUN_1885 {ECO:0000313|EMBL:BAF72832.1};
OS Sulfurovum sp. (strain NBC37-1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurovaceae; Sulfurovum.
OX NCBI_TaxID=387093 {ECO:0000313|EMBL:BAF72832.1, ECO:0000313|Proteomes:UP000006378};
RN [1] {ECO:0000313|EMBL:BAF72832.1, ECO:0000313|Proteomes:UP000006378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBC37-1 {ECO:0000313|EMBL:BAF72832.1,
RC ECO:0000313|Proteomes:UP000006378};
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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; AP009179; BAF72832.1; -; Genomic_DNA.
DR RefSeq; WP_012083645.1; NC_009663.1.
DR AlphaFoldDB; A6QBH3; -.
DR STRING; 387093.SUN_1885; -.
DR KEGG; sun:SUN_1885; -.
DR eggNOG; COG1376; Bacteria.
DR HOGENOM; CLU_1414529_0_0_7; -.
DR OrthoDB; 9786799at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000006378; 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 Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..211
FT /note="L,D-transpeptidase catalytic domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002698465"
FT DOMAIN 52..167
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 211 AA; 23734 MW; FF3C5D2D6F3B7B53 CRC64;
MKKFLLMSIG WMLLTQLAFA GDPASKVFPL SKSRFAVVHN GQEKIVDLSG QDYIVVSLRE
EGADGIAYAI DRDGVVWWAA SISSGAKGHE TPSGIFPIFR KERFYMSKAH PDPKGINNMD
FSLWFTSQGH AIHMGNDDGM SHGCIHVGKK GAATMFKWAK KGTKVVVTRE HYLPFVYYDL
RKSGYKESKV KKGYIKQYLK TMKPVKPHMP E
//
