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Database: UniProt
Entry: A0A323UXL3_9RHOO
LinkDB: A0A323UXL3_9RHOO
Original site: A0A323UXL3_9RHOO 
ID   A0A323UXL3_9RHOO        Unreviewed;       564 AA.
AC   A0A323UXL3;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   02-APR-2025, entry version 21.
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; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Rhodocyclales; Zoogloeaceae; 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, ECO:0000256|PROSITE-ProRule:PRU01373}.
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:UniProtKB-ARBA.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-UniRule.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
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; 1.
DR   InterPro; IPR052905; LD-transpeptidase_YkuD-like.
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.
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   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984,
KW   ECO:0000256|PROSITE-ProRule:PRU01373};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248259};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          328..498
FT                   /note="L,D-TPase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS52029"
FT   ACT_SITE        456
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01373"
FT   ACT_SITE        475
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01373"
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
//
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