ID   A0A1R4HWL8_9GAMM        Unreviewed;       373 AA.
AC   A0A1R4HWL8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=ErfK/YbiS/YcfS/YnhG family protein {ECO:0000313|EMBL:SJN11935.1};
GN   ORFNames=CZ787_06980 {ECO:0000313|EMBL:SJN11935.1};
OS   Halomonas sp. JB380.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1434831 {ECO:0000313|EMBL:SJN11935.1, ECO:0000313|Proteomes:UP000196331};
RN   [1] {ECO:0000313|Proteomes:UP000196331}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB380 {ECO:0000313|Proteomes:UP000196331};
RA   Dridi B.;
RL   Submitted (FEB-2017) 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; FUKM01000028; SJN11935.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R4HWL8; -.
DR   OrthoDB; 9787225at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000196331; 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; cd00118; LysM; 1.
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; IPR018392; LysM_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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..373
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012955410"
FT   DOMAIN          136..268
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
FT   REGION          342..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..373
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   373 AA;  40580 MW;  30E31354431302D2 CRC64;
     MNIRHKFNLW GPTSLAVLLA ASLTGPAYAQ TASEQAENAP AIADESVASA EQITDARELP
     RGHFRLPDQG DIIGESYTIT VDDPAETLID IARRHNIGYE EIRMANPGVS MWVPGEGTEI
     VIPAQYILPP APREGVVVNL SELRLYYYPA NNPGIVETYP VSVGREEFAT PVGITRTTIK
     VKDPAWAPPA SMRREAAARG EPAPSVVPAG PNNPLGEHAI LLAMPSYLIH GTNRPDGVGM
     RASRGCIRMY PEDIKSLYER LPSGTQVNLM DAPFKAGWAA DGTLFVQSYP QLEENVGDFE
     PLLDAIDRVD ALTEDQVAVD YAKVKSAVES PNGRFVALYG PQAQPTVEEE PASRNSLLEE
     VELSHRQMTE EDA
//