ID A0A0Q9M543_9BACL Unreviewed; 493 AA.
AC A0A0Q9M543;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=L,D-transpeptidase catalytic domain-containing protein {ECO:0000259|Pfam:PF03734};
GN ORFNames=ASL11_25585 {ECO:0000313|EMBL:KRE59605.1};
OS Paenibacillus sp. Soil750.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736398 {ECO:0000313|EMBL:KRE59605.1, ECO:0000313|Proteomes:UP000051252};
RN [1] {ECO:0000313|EMBL:KRE59605.1, ECO:0000313|Proteomes:UP000051252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil750 {ECO:0000313|EMBL:KRE59605.1,
RC ECO:0000313|Proteomes:UP000051252};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE59605.1, ECO:0000313|Proteomes:UP000051252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil750 {ECO:0000313|EMBL:KRE59605.1,
RC ECO:0000313|Proteomes:UP000051252};
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:KRE59605.1}.
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DR EMBL; LMSD01000034; KRE59605.1; -; Genomic_DNA.
DR RefSeq; WP_056621165.1; NZ_LMSD01000034.1.
DR AlphaFoldDB; A0A0Q9M543; -.
DR STRING; 1736398.ASL11_25585; -.
DR OrthoDB; 9787225at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000051252; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR005490; LD_TPept_cat_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
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; PF07719; TPR_2; 1.
DR Pfam; PF03734; YkuD; 1.
DR SMART; SM00028; TPR; 1.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 119..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 45..78
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 347..453
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 493 AA; 55534 MW; 1229AFEC120B0D44 CRC64;
MIRRNQRFRN QLDDHLVHLH KNLFISHADP LYHEKVIRYL DANSPEAHFN LGQKFREKGN
WKRARFHYKE ALKTYPSPFY SAANRAIHLL DQQQATHVAN LEQTLPEKRK PLLPPFMKML
LLVLLILNVL LVLFFAGDQA IPRTISKMKL WSSGTQVTYE SVDKPFILYL SPEMSHAEIE
KKLHAQALVL AKEIPKSTIL LYGIITEDNV DKGKTMLLTN EDDIKRAMVI ATYQPEADAL
VHIRFLNAEF EEHQPLSAIG ANLVRTALDS YRDNVGQAPT RIDELLQDYP LNYLSFIPIE
TLSGSNEIKS AYKGDGGWVF NPKAADIAHM FYANVVGGDE VPYEPVHLEV SQRDYQLQLV
SGSYLLWDKE IGLGANGSTP DGVYRVIERV QQPKGKTSQS YGDAGLGLGS IALHGTYDES
SIGEAKSLGC IRLTNDDIQQ LFPFVPKGTE VRILSSEHTP IRVDQVGQMS KLIPTSLPQH
SESAGNTIFH WLG
//
