ID A0A2S5JKF6_9RHOB Unreviewed; 577 AA.
AC A0A2S5JKF6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Murein L,D-transpeptidase YcbB/YkuD {ECO:0000313|EMBL:PPB81881.1};
GN ORFNames=LV82_01098 {ECO:0000313|EMBL:PPB81881.1};
OS Albidovulum inexpectatum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Albidovulum.
OX NCBI_TaxID=196587 {ECO:0000313|EMBL:PPB81881.1, ECO:0000313|Proteomes:UP000239736};
RN [1] {ECO:0000313|EMBL:PPB81881.1, ECO:0000313|Proteomes:UP000239736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12048 {ECO:0000313|EMBL:PPB81881.1,
RC ECO:0000313|Proteomes:UP000239736};
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 (JAN-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:PPB81881.1}.
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DR EMBL; PRDS01000002; PPB81881.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5JKF6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000239736; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000239736};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 45..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 90..225
FT /note="L,D-transpeptidase scaffold"
FT /evidence="ECO:0000259|Pfam:PF20142"
FT DOMAIN 252..306
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 337..497
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 577 AA; 64826 MW; 2EDE7BCD790BA123 CRC64;
MPVDGLGHRN ARESNHKWFS GAGMSLGLIG FLSTRGWVVR RVSRAAAIAL GVALGAGIVQ
PVAAQEEKAL RVPDLSYRLA LAEAAAGRPA IARFYREHDY AALWTAPEAQ VRRGALISAL
ERAEEHGLPS FAPRSRDLLA RLGAMQTQAD RAQLEVAMSA AFLDYARALH SGVLTPAKVD
PGIVREVPRL DPLKLLQDFA RSEPRAYLRA LAPQVPQYDQ LRRAMLDLRE VIAAGGWGPA
VPGGKKLAPG DTGARVVALR DRLIRMDYLR PTLSAVYERE IQKAVQQFQL DHGLTPDGIA
GPSTLAEINV GPEERLRSVL VALERLRWMN GLDLGERHVW VNIPDFTAKV IDDGKQRFET
ITVVGKDQPD RRSPEFSDLM EYMVINPTWN VPRSIAVKEY LPKLKKNPNA VRHLRITDRR
GRVIDRSKVD FTQFTARNFP FNMSQPPDDD NALGLVKFMF PNPWNIYLHD TPSKSLFSRE
VRAFSHGCIR LGQPFEFAYV LLERQSDDPK VEFHRHLRTG RETTVPLEQP VPVHIVYFTA
WPDRFGQVRF RRDVYGRDGR IFDALRAAGL EFDALRG
//