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Database: UniProt
Entry: A0A420DPC7_9RHOB
LinkDB: A0A420DPC7_9RHOB
Original site: A0A420DPC7_9RHOB 
ID   A0A420DPC7_9RHOB        Unreviewed;       188 AA.
AC   A0A420DPC7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Lipoprotein-anchoring transpeptidase ErfK/SrfK {ECO:0000313|EMBL:RKE96050.1};
GN   ORFNames=C8N30_0601 {ECO:0000313|EMBL:RKE96050.1};
OS   Sulfitobacter guttiformis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Sulfitobacter.
OX   NCBI_TaxID=74349 {ECO:0000313|EMBL:RKE96050.1, ECO:0000313|Proteomes:UP000284407};
RN   [1] {ECO:0000313|EMBL:RKE96050.1, ECO:0000313|Proteomes:UP000284407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11458 {ECO:0000313|EMBL:RKE96050.1,
RC   ECO:0000313|Proteomes:UP000284407};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   -!- SIMILARITY: Belongs to the YkuD family.
CC       {ECO:0000256|ARBA:ARBA00005992}.
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:RKE96050.1}.
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DR   EMBL; RAQK01000001; RKE96050.1; -; Genomic_DNA.
DR   RefSeq; WP_025063002.1; NZ_RAQK01000001.1.
DR   AlphaFoldDB; A0A420DPC7; -.
DR   STRING; 1443111.Z949_2577; -.
DR   OrthoDB; 9795305at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000284407; Unassembled WGS sequence.
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; IPR038063; Transpep_catalytic_dom.
DR   PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR   Pfam; PF03734; YkuD; 1.
DR   SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
PE   3: Inferred from homology;
KW   Lipoprotein {ECO:0000313|EMBL:RKE96050.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000284407};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..188
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019478234"
FT   DOMAIN          59..186
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
SQ   SEQUENCE   188 AA;  21188 MW;  E40BB08F19318546 CRC64;
     MTNKPFSRRR MILAAGASLA LPSLVRAQDA PDIVENRRNI MSFRTQRWQD HFETLGKGAI
     VADISSRTLH YWDADGVTYK IYPSSVPRSE ELTKRGYTQI VRKRVGPDWT PTASMMERDP
     TLAYMPPGPG NPLGTHAMYL SWPAYLIHGT HDTRKIGRQS SDGCIGLYNH KVEELFAMAQ
     VGTQVRLV
//
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