ID A0A3S9T045_9FIRM Unreviewed; 384 AA.
AC A0A3S9T045;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JAN-2026, entry version 22.
DE RecName: Full=L,D-TPase catalytic domain-containing protein {ECO:0000259|PROSITE:PS52029};
GN ORFNames=BBF96_10580 {ECO:0000313|EMBL:AZR73792.1};
OS Anoxybacter fermentans.
OC Bacteria; Bacillati; Bacillota; Clostridia; Halanaerobiales; Anoxybacter.
OX NCBI_TaxID=1323375 {ECO:0000313|EMBL:AZR73792.1, ECO:0000313|Proteomes:UP000267250};
RN [1] {ECO:0000313|EMBL:AZR73792.1, ECO:0000313|Proteomes:UP000267250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY22613 {ECO:0000313|EMBL:AZR73792.1,
RC ECO:0000313|Proteomes:UP000267250};
RA Zeng X., Shao Z.;
RT "Genome and transcriptome analysis of iron-reducing fermentative bacteria
RT Anoxybacter fermentans.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|PROSITE-ProRule:PRU01373}.
CC -!- SIMILARITY: Belongs to the YkuD family.
CC {ECO:0000256|ARBA:ARBA00005992}.
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DR EMBL; CP016379; AZR73792.1; -; Genomic_DNA.
DR RefSeq; WP_127017139.1; NZ_CP016379.1.
DR AlphaFoldDB; A0A3S9T045; -.
DR KEGG; aft:BBF96_10580; -.
DR OrthoDB; 9787225at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000267250; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:TreeGrafter.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0071972; F:peptidoglycan L,D-transpeptidase activity; IEA:TreeGrafter.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-UniRule.
DR GO; GO:0018104; P:peptidoglycan-protein cross-linking; IEA:TreeGrafter.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-UniRule.
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; 2.
DR InterPro; IPR050979; LD-transpeptidase.
DR InterPro; IPR005490; LD_TPept_cat_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; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30582:SF24; L,D-TRANSPEPTIDASE ERFK_SRFK-RELATED; 1.
DR Pfam; PF01471; PG_binding_1; 2.
DR Pfam; PF03734; YkuD; 1.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR SUPFAM; SSF47090; PGBD-like; 2.
DR PROSITE; PS52029; LD_TPASE; 1.
PE 3: Inferred from homology;
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|PROSITE-
KW ProRule:PRU01373};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|PROSITE-ProRule:PRU01373};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984,
KW ECO:0000256|PROSITE-ProRule:PRU01373};
KW Reference proteome {ECO:0000313|Proteomes:UP000267250};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 196..304
FT /note="L,D-TPase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS52029"
FT ACT_SITE 264
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01373"
FT ACT_SITE 280
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01373"
SQ SEQUENCE 384 AA; 44443 MW; 9A3EB5CC329F5793 CRC64;
MKTIKFKKWI VLIFVFIFIL TFTFTYIFYL DKKPLVSDDQ KNRNKIIEES AIDQMDIQFK
KQNQNLSLEP AANLEDIIKA SKDLFLLKHM IENGQEWIKG ELENYPVLKY SEPMLRNDDV
KGVQAILKKL DFYYGAIDGI YGPKTLAAVK KLQKRYGLKP TGIMDLDDYN LLARVYEENI
EENIPVVGKS KPEGKVSILI VLDERTLYVF EDNKIFAKFP VAIGKRDTPS PIGNWKIISK
DSWGGGFGTH WLGLNVPYGK YGIHGTNKPW SIGTAASHGC FRMFNRDIET LYKWVTWGTR
VFVVGGNFPY NLPWRTINDG DRGSDVWMVQ NRLRELGYYK WRPDGIFGYR TKKAVQRFQK
DYGLPADGEV GWSTLQKLGF YLFQ
//
