ID   A0A1I2XUM7_9RHOB        Unreviewed;       249 AA.
AC   A0A1I2XUM7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Lipoprotein-anchoring transpeptidase ErfK/SrfK {ECO:0000313|EMBL:SFH17163.1};
GN   ORFNames=SAMN04488021_102120 {ECO:0000313|EMBL:SFH17163.1};
OS   Paracoccus aminovorans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=34004 {ECO:0000313|EMBL:SFH17163.1, ECO:0000313|Proteomes:UP000183635};
RN   [1] {ECO:0000313|EMBL:SFH17163.1, ECO:0000313|Proteomes:UP000183635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8537 {ECO:0000313|EMBL:SFH17163.1,
RC   ECO:0000313|Proteomes:UP000183635};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOPU01000002; SFH17163.1; -; Genomic_DNA.
DR   RefSeq; WP_074966099.1; NZ_LN832559.1.
DR   AlphaFoldDB; A0A1I2XUM7; -.
DR   STRING; 34004.SAMN04488021_102120; -.
DR   OrthoDB; 9795305at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000183635; 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   PANTHER; PTHR30582:SF24; L,D-TRANSPEPTIDASE ERFK_SRFK-RELATED; 1.
DR   Pfam; PF03734; YkuD; 1.
DR   SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipoprotein {ECO:0000313|EMBL:SFH17163.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183635};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..249
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010220520"
FT   DOMAIN          77..212
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
FT   REGION          22..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   249 AA;  26417 MW;  D90581D5C5B2819E CRC64;
     MRLAPLMLAL GLGLAACAPT PQTPSAPPAA DQGVYGARTD SGPNGEPIEI HAVRPAYLTD
     RNRRQLVPYN GPEAAGTIVV DPYARFLYHV QGDGQAMRYG VAVGQAGKNF QGNATVGRKH
     AWPSWTPTAN MVRTQPELYG PLKGGLRGGV DNPLGSRALY LYKGGRDTMY RIHGTMDPSS
     IGKATSAGCI RLFNQDIMDL FNEIPSGTQV KVRTRAESLA LEGPLVEQPN GYLAPAGGEM
     QTAEASAAQ
//