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Database: UniProt
Entry: A0A146GAI0_TERSA
LinkDB: A0A146GAI0_TERSA
Original site: A0A146GAI0_TERSA 
ID   A0A146GAI0_TERSA        Unreviewed;       211 AA.
AC   A0A146GAI0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Lipoprotein-anchoring transpeptidase ErfK/SrfK {ECO:0000313|EMBL:GAT33797.1};
GN   ORFNames=TSACC_22215 {ECO:0000313|EMBL:GAT33797.1};
OS   Terrimicrobium sacchariphilum.
OC   Bacteria; Verrucomicrobiota; Terrimicrobiia; Terrimicrobiales;
OC   Terrimicrobiaceae; Terrimicrobium.
OX   NCBI_TaxID=690879 {ECO:0000313|EMBL:GAT33797.1, ECO:0000313|Proteomes:UP000076023};
RN   [1] {ECO:0000313|Proteomes:UP000076023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NM-5 {ECO:0000313|Proteomes:UP000076023};
RA   Qiu Y., Matsuura N., Ohashi A., Tourlousse M.D., Sekiguchi Y.;
RT   "Draft genome sequence of Terrimicrobium sacchariphilum strain NM-5.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000076023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NM-5 {ECO:0000313|Proteomes:UP000076023};
RA   Qiu Y.-L., Tourlousse D.M., Matsuura N., Ohashi A., Sekiguchi Y.;
RT   "Draft genome sequence of Terrimicrobium sacchariphilum NM-5(T), a
RT   facultative anaerobic soil bacterium of the class Spartobacteria.";
RL   Genome Announc. 0:0-0(2017).
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
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:GAT33797.1}.
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DR   EMBL; BDCO01000002; GAT33797.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A146GAI0; -.
DR   STRING; 690879.TSACC_22215; -.
DR   InParanoid; A0A146GAI0; -.
DR   OrthoDB; 177750at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000076023; Unassembled WGS sequence.
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   Lipoprotein {ECO:0000313|EMBL:GAT33797.1};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..211
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007524661"
FT   DOMAIN          73..209
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
SQ   SEQUENCE   211 AA;  22626 MW;  06C76DC0FD23DCAB CRC64;
     MTVALPHIRV KETAAILIAA AVLVVSQAAA QQGGAAAPTP RPKQKKASEL IYKQEPPRIF
     ERVLEKSTPA NSTIVISLGK QRAYFLVDGE TAIDSPISSG KRAGMTPKGT YKISEKDADH
     RSSVYGDFVS QRTGKTVRAG VSTKIDSAPS GTVYRGAPMR WFMRLTNDGV GMHTGILPGY
     PASHGCIRLP EEIAKLFYSK VVLGTQVTVT D
//
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