ID A0A2R8AWN0_9RHOB Unreviewed; 537 AA.
AC A0A2R8AWN0;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Murein L,D-transpeptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PRI8871_02258 {ECO:0000313|EMBL:SPF80452.1};
OS Pseudoprimorskyibacter insulae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudoprimorskyibacter.
OX NCBI_TaxID=1695997 {ECO:0000313|EMBL:SPF80452.1, ECO:0000313|Proteomes:UP000244904};
RN [1] {ECO:0000313|Proteomes:UP000244904}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8871 {ECO:0000313|Proteomes:UP000244904};
RA Rodrigo-Torres L., Arahal R. D., Lucena T.;
RL Submitted (MAR-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}.
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DR EMBL; OMOJ01000004; SPF80452.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R8AWN0; -.
DR OrthoDB; 9778545at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000244904; 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: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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000244904};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..537
FT /note="Murein L,D-transpeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015334469"
FT DOMAIN 50..185
FT /note="L,D-transpeptidase scaffold"
FT /evidence="ECO:0000259|Pfam:PF20142"
FT DOMAIN 212..266
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 298..461
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 537 AA; 60068 MW; B8F2018AC284B047 CRC64;
MKIALKIRHC TFGLLTATAL AAFVPGAPVQ AQVTAFKQAV AETAARHDGV ADFYRERVFE
PIWTGDDDAS RARRAAFLRA MTTSHLHGLP ERRFDPKAIL AMMQGQKSSR DLGKLEVELS
IAFADFASAL QTGILEPKRI DDGLVRKVPR RSPAEHLRGL TTQDPDVFFR SLVPPSPEYS
RLMKAKFRME RQLSTGGWGA TVPASSLKPG NSGKAVVALR DRLVRMGYMG RSASAEYDGT
LQAAVRQFQE DHGLEADGVA GASTIKEVNI GVEERLEQIM VAMERERWLN FPEGLGKRHV
KVNLTDFKAW IIDDDKVTFE TRAVVGMNQS DRRTPEFSDE MERMVINPSW YVPRSIIVNE
YLPALRSNPN SVGHLEITDA RGRVVNRGNG FSQYSAQSFP FAMRQPPGPK NALGLVKFLF
PNKYNIYLHD TPAKSLFSRE VRAYSHGCIR LHKPQEFAHA ILAPQVSNPK EYFERILRTG
AETPVELDQH VPVHLMYRTA YTDVKGVMQY RNDVYGRDAK IWRALSAEGV TVGAVQG
//
