ID A0A1X6YZU9_9RHOB Unreviewed; 538 AA.
AC A0A1X6YZU9;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 02-APR-2025, entry version 24.
DE SubName: Full=Murein L,D-transpeptidase {ECO:0000313|EMBL:SLN36006.1};
GN ORFNames=ROA7450_01703 {ECO:0000313|EMBL:SLN36006.1};
OS Roseovarius albus.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1247867 {ECO:0000313|EMBL:SLN36006.1, ECO:0000313|Proteomes:UP000193061};
RN [1] {ECO:0000313|EMBL:SLN36006.1, ECO:0000313|Proteomes:UP000193061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7450 {ECO:0000313|EMBL:SLN36006.1,
RC ECO:0000313|Proteomes:UP000193061};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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; FWFX01000004; SLN36006.1; -; Genomic_DNA.
DR RefSeq; WP_143534403.1; NZ_FWFX01000004.1.
DR AlphaFoldDB; A0A1X6YZU9; -.
DR OrthoDB; 9778545at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000193061; 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:UP000193061};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..538
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013276321"
FT DOMAIN 298..474
FT /note="L,D-TPase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS52029"
FT ACT_SITE 430
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01373"
FT ACT_SITE 449
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01373"
SQ SEQUENCE 538 AA; 60857 MW; 06CD38419C5AB00F CRC64;
MTRKPPINRV TKLACVLWAS VATTFFEPNS ALAQSTAFRQ AIAEHAASDR ALATFFQEHD
YQRFWTVQGE IGTKRRAALF RAIEGAELHG LPAARYDTQN VMQQLEAAKS PRDLGQIEVA
MSGLLLDYAR DLKTGVLVPG AVDGSIKRER PSFDQKAVLA AFASGNPNAL ITELAPDSNE
YRRLMKEKLR LENLIQMGGW GPAVQAEKLE EGDAGNTVIA LRNRLMSMEY LERHVGVVYD
QKIKQAVQAF QLANGLEPDG VAGPSTLAEL NKSVEDRLKS IIVAMERERW ISQPRNERHI
RVNLTDFHAR VYENDEVQFE TRAVVGKNGD DRRSPEFSDE MEFMVINPTW HVPRSIAVKE
YLPKLKRNRN AVSHLKIYNR QGRVVNRGAI NFAAFNKRNF PFAIKQPPSE KNALGLVKFM
FPNKYNIYLH DTPAKDLFAR EKRDFSHGCI RLQKPFGFAY EMLSKQENDP KAFFHRKLDT
GKETKVLLDQ KVPVHIIYRT AFTLPKEGVQ FRSDVYGRDA KIWDALSKAG VSLGAVQG
//
