ID   A0A1H3ASK2_9GAMM        Unreviewed;       389 AA.
AC   A0A1H3ASK2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=L,D-transpeptidase ErfK/SrfK {ECO:0000313|EMBL:SDX32623.1};
GN   ORFNames=SAMN05443545_10517 {ECO:0000313|EMBL:SDX32623.1};
OS   Aidingimonas halophila.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Aidingimonas.
OX   NCBI_TaxID=574349 {ECO:0000313|EMBL:SDX32623.1, ECO:0000313|Proteomes:UP000198500};
RN   [1] {ECO:0000313|EMBL:SDX32623.1, ECO:0000313|Proteomes:UP000198500}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19219 {ECO:0000313|EMBL:SDX32623.1,
RC   ECO:0000313|Proteomes:UP000198500};
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; FNNI01000005; SDX32623.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3ASK2; -.
DR   STRING; 574349.SAMN05443545_10517; -.
DR   OrthoDB; 9787225at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000198500; 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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198500};
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..389
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011558491"
FT   DOMAIN          133..270
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
FT   REGION          35..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          168..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..202
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   389 AA;  43318 MW;  E0232F778EEA31F5 CRC64;
     MARLRQRLPG RFTVPGLSCA LLTAMLVISA PTTAWAQDDE KASRPDDVPE QDEQEQQGTR
     LVYPIPEDGD VVGEVQTVIA DEDDTLIDIG RAHGLGYEEM RRANPGLSMW YPGEGAEVVL
     PKRFILPPGP REGIVINLSE LRLYYYPEVE EGETPVVETY PISVGREGFS TPLGETRTTM
     KVKDPSWSPP ESMRREAAER GDPPPEIVPP GPDNPLGRHA VLLDIPGYLI HGTNRPDGVG
     MRVSRGCVRL YPENIEYLYE NLPNNTQVRI INEPFKVGWS DDMLYVQSYP LLKDDDIAFE
     PIINAVDAVD DVMKEADGDS PPVDYARVRY AIDASRGQPE PVLSSAPLLV DTAPVEALDL
     RTDFFREIDT DATWSDRSTL YDALELSER
//