ID G2IRF8_SPHSK Unreviewed; 415 AA.
AC G2IRF8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:BAK68524.1};
GN ORFNames=SLG_38490 {ECO:0000313|EMBL:BAK68524.1};
OS Sphingobium sp. (strain NBRC 103272 / SYK-6).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=627192 {ECO:0000313|EMBL:BAK68524.1, ECO:0000313|Proteomes:UP000001275};
RN [1] {ECO:0000313|EMBL:BAK68524.1, ECO:0000313|Proteomes:UP000001275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 103272 / SYK-6 {ECO:0000313|Proteomes:UP000001275};
RX PubMed=22207743; DOI=10.1128/JB.06254-11;
RA Masai E., Kamimura N., Kasai D., Oguchi A., Ankai A., Fukui S.,
RA Takahashi M., Yashiro I., Sasaki H., Harada T., Nakamura S., Katano Y.,
RA Narita-Yamada S., Nakazawa H., Hara H., Katayama Y., Fukuda M.,
RA Yamazaki S., Fujita N.;
RT "Complete genome sequence of Sphingobium sp. strain SYK-6, a degrader of
RT lignin-derived biaryls and monoaryls.";
RL J. Bacteriol. 194:534-535(2012).
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; AP012222; BAK68524.1; -; Genomic_DNA.
DR AlphaFoldDB; G2IRF8; -.
DR STRING; 627192.SLG_38490; -.
DR KEGG; ssy:SLG_38490; -.
DR eggNOG; COG2989; Bacteria.
DR HOGENOM; CLU_020360_4_0_5; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001275; Chromosome.
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; IPR045380; LD_TPept_scaffold_dom.
DR InterPro; IPR038063; Transpep_catalytic_dom.
DR PANTHER; PTHR41533:SF2; BLR7131 PROTEIN; 1.
DR PANTHER; PTHR41533; L,D-TRANSPEPTIDASE HI_1667-RELATED; 1.
DR Pfam; PF20142; Scaffold; 1.
DR Pfam; PF03734; YkuD; 1.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001275};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..36
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 37..415
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003432053"
FT DOMAIN 43..156
FT /note="L,D-transpeptidase scaffold"
FT /evidence="ECO:0000259|Pfam:PF20142"
FT DOMAIN 187..337
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 415 AA; 45320 MW; 64C725A9402FA5C5 CRC64;
MLQGSAQPLP DDWRFSVRIL ILALSFLLCV APPAHAATPW TVQAAARLLD YGEKIGTHGL
DPADYELDRL RTALAARDQT ALDTAATRSF ALLARDLANG RVPAAQRRLS YFRTANLTPD
AVLELLDRAL ATGDVPGTLD RLAPANADYR MLRAALASLP ADARSDRARV RANLERWRWL
PRDLGERYLL VNVPEYVVRL MDGGKSVAEH RVIVGKRATP TPQFATTATG IIFNPTWTVP
QSIIRESVGA LVRNRPDTAR ARGYTWTGSG ANLHVVQQPG PTNSLGQMKI DMPNPLSIFL
HDTPSKTLFG QETRMFSHGC VRTDRPFDLA ARMLAGTEWT PGRIEEAVAA RETITAKLPR
PVAVFVIYMT ARADADGRLH SFDDIYGLDA GISRDLGVAG LAAVRQLSDR TCAAG
//
