ID A0A0Q6Z4R2_9BRAD Unreviewed; 519 AA.
AC A0A0Q6Z4R2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=L,D-transpeptidase catalytic domain-containing protein {ECO:0000259|Pfam:PF03734};
GN ORFNames=ASC80_12205 {ECO:0000313|EMBL:KQW20923.1};
OS Afipia sp. Root123D2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=1736436 {ECO:0000313|EMBL:KQW20923.1, ECO:0000313|Proteomes:UP000051348};
RN [1] {ECO:0000313|EMBL:KQW20923.1, ECO:0000313|Proteomes:UP000051348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW20923.1,
RC ECO:0000313|Proteomes:UP000051348};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW20923.1, ECO:0000313|Proteomes:UP000051348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW20923.1,
RC ECO:0000313|Proteomes:UP000051348};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQW20923.1}.
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DR EMBL; LMDP01000002; KQW20923.1; -; Genomic_DNA.
DR RefSeq; WP_056297273.1; NZ_LMDP01000002.1.
DR AlphaFoldDB; A0A0Q6Z4R2; -.
DR STRING; 1736436.ASC80_12205; -.
DR OrthoDB; 463216at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000051348; 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 InterPro; IPR016915; UCP029342.
DR PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30582:SF34; L,D-TRANSPEPTIDASE YCIB-RELATED; 1.
DR Pfam; PF03734; YkuD; 1.
DR PIRSF; PIRSF029342; UCP029342_ErfK/YbiS/YcfS/YnhG; 2.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000051348};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..519
FT /note="L,D-transpeptidase catalytic domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006299637"
FT DOMAIN 63..169
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 494..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 236..286
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 519 AA; 55698 MW; F7D611A0A3F252EC CRC64;
MVDRLTSAKS TVAMRHWGFS AVVMFAAMVA LMAPTADAAA KQARRAQPAE TAAPREAGEP
IMAIVSIKSQ QVTFYDAEGW ILRAPVSTGV NGRETPAGVF AIVEKDKDHH STMYDDAWMP
NMLRITWNGL ALHGGPLPGY AASHGCVRMP YGFAEKLFDK TRIGMRVIIS PDDAAPVDFS
HPALSLFVPN TEVVAAAPAK AEMLSREAAD AATSAAEAKK TAVTAARESA PLAASLRKLE
RLKARADAKL VSADKAVAAA RTDQARAKAE DRRQKAAAKA AELGIQFDTA KTNASSKLDA
ASAAKEAAKT AQTKKADAAK AALDAKLALE PVSIYISRAT RTLYVRRNTH KPAPDGGGEV
FDATIEVPVT IRDPGKPLGT HVFTAVARND AGLRWTAVTV ENREDAKSAL DRITIPKEVL
DRIAPTALPR SSIVVSDEPL SEETNYRTEF VAVLSDQPQG GFITRKPSEV LMVDDNDWGN
GNWRDDDGFG FFLQRNPGPQ PRNTRRGGGQ LFPPEQPGW
//
