ID   A0A1J0VHS7_9GAMM        Unreviewed;       537 AA.
AC   A0A1J0VHS7;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Murein L,D-transpeptidase {ECO:0000313|EMBL:APE31587.1};
GN   ORFNames=BOX17_11885 {ECO:0000313|EMBL:APE31587.1};
OS   Halomonas aestuarii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1897729 {ECO:0000313|EMBL:APE31587.1, ECO:0000313|Proteomes:UP000181985};
RN   [1] {ECO:0000313|Proteomes:UP000181985}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hb3 {ECO:0000313|Proteomes:UP000181985};
RA   Koh H.-W., Rani S., Park S.-J.;
RT   "Halolamina sediminis sp. nov., an extremely halophilic archaeon isolated
RT   from solar salt.";
RL   Submitted (NOV-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; CP018139; APE31587.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J0VHS7; -.
DR   KEGG; hsi:BOX17_11885; -.
DR   OrthoDB; 9778545at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000181985; Chromosome.
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   Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR   InterPro; IPR005490; LD_TPept_cat_dom.
DR   InterPro; IPR045380; LD_TPept_scaffold_dom.
DR   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
DR   InterPro; IPR038063; Transpep_catalytic_dom.
DR   PANTHER; PTHR41533:SF2; BLR7131 PROTEIN; 1.
DR   PANTHER; PTHR41533; L,D-TRANSPEPTIDASE HI_1667-RELATED; 1.
DR   Pfam; PF01471; PG_binding_1; 1.
DR   Pfam; PF20142; Scaffold; 1.
DR   Pfam; PF03734; YkuD; 1.
DR   SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR   SUPFAM; SSF47090; PGBD-like; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..537
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012181771"
FT   DOMAIN          47..185
FT                   /note="L,D-transpeptidase scaffold"
FT                   /evidence="ECO:0000259|Pfam:PF20142"
FT   DOMAIN          214..281
FT                   /note="Peptidoglycan binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF01471"
FT   DOMAIN          310..469
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
SQ   SEQUENCE   537 AA;  60815 MW;  FB55D6B761A5CB01 CRC64;
     MPSAIGLKPL ILAGVMALSL ATAALAEDAP PPQADSLLER LDEQEGALRD FYAVREGRPA
     WQDVATVADF AAALRTLDTD GLNPLDYRPD ALVTAHRQVY AEGSTPADRA RFDLQASRVL
     LTALRHLQRG KVDPYRIDPD WEVPIEAPPL DLPAISRAVD AHRFEQAFAA ARPSAPPYER
     LRAGLARYRH IERQGGWPML PLRPEPLRPG DLHEDVPLLR ERLAIMGELE VMVADLFAGV
     ESRDTDPRRY DERLVEAVKE FQQRHLLEVD GIIGPQTREA LNVPVSRRID QIRVNLERAR
     WLLHGLPDSF VLVDIAGYRI SYFRPDGDVW RSRIVVGRPY RRTPSLRSRI TYLTLNPTWT
     VPPTILREDV LPGVRRDLGY LWEHDLMVLS PSGQRLDPRE VNWWHPGNVI LRQRSGPQNA
     LGRVVLRFPN DHLVYLHDTP AQGLFAREQR AFSSGCIRVQ GVLQLAQYLF DDTGTPAHVA
     TLVSEGVTRN ISLERPVPVI LHYWTVDPSE DGRLVFRPDI YERDAALREA LDRPLPR
//