ID A0A323UXL3_9RHOO Unreviewed; 564 AA.
AC A0A323UXL3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Murein L,D-transpeptidase {ECO:0000313|EMBL:PZA17215.1};
GN ORFNames=DNK49_08275 {ECO:0000313|EMBL:PZA17215.1};
OS Parazoarcus communis SWub3 = DSM 12120.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Parazoarcus.
OX NCBI_TaxID=1121029 {ECO:0000313|EMBL:PZA17215.1, ECO:0000313|Proteomes:UP000248259};
RN [1] {ECO:0000313|EMBL:PZA17215.1, ECO:0000313|Proteomes:UP000248259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SWub3 {ECO:0000313|EMBL:PZA17215.1,
RC ECO:0000313|Proteomes:UP000248259};
RA Zorraquino Salvo V., Toubiana D., Blumwald E.;
RT "Azoarcus communis strain SWub3 genome.";
RL Submitted (JUN-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:PZA17215.1}.
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DR EMBL; QKOE01000004; PZA17215.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A323UXL3; -.
DR OrthoDB; 9778545at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000248259; 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 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; L,D-TRANSPEPTIDASE HI_1667-RELATED; 1.
DR PANTHER; PTHR41533:SF1; L,D-TRANSPEPTIDASE YCBB-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 Reference proteome {ECO:0000313|Proteomes:UP000248259};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 82..217
FT /note="L,D-transpeptidase scaffold"
FT /evidence="ECO:0000259|Pfam:PF20142"
FT DOMAIN 264..300
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 328..489
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 564 AA; 62750 MW; D8F0B055C1570C00 CRC64;
MSISLESIRW CRSFCTNRPN LIRQSMNSQM EKRANLTIRA ILLICMVFSA LQTVRAANAD
EALRDAIRQT FEAAPELRET DVSGVYARRA YTPLWQSPTR REQLLTALAD LTHDGLDPEH
YALSQLRQDF AHASNTEHRL AAELAATRNC LLALTHLQHG VLDPVRDGGY WRGPNGAAPT
LPAATEALAA LADNDLDALF ARFRPSTPLY LKLREALITA RQAAPNAWPQ VPAGLTIKPG
KRDDRLPGLR TRLIASRHLG SEHAAGDQMD DALVEAVKTF QRENGLEADG AVGPATLHAL
NMTREARLSS LRINLERARW IAPHQRGNHV MVDVTGYRLS YFSDQTERWH ARTQVGMPSR
ETPELFSRIT HLTVNPTWTV PPTILKKDIV PKASTDPNYL ASRNIRVFDR DGTELDPATV
DWSRPGNLTL RQDFGDGSAL GKVAIRFANP YAIYLHDTPN QRQFRRAQRT FSSGCVRVEN
ALDLVQLLLE PGGDSHLARF DKALTSGRTG NLNLPQPVPI IVAYLTAGPD DNGRIVFRQD
IYKRDAMLSA KLDQAGKSIA DKKL
//
