ID B5ZRL8_RHILW Unreviewed; 636 AA.
AC B5ZRL8;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Peptidoglycan-binding domain 1 protein {ECO:0000313|EMBL:ACI55299.1};
DE Flags: Precursor;
GN OrderedLocusNames=Rleg2_2015 {ECO:0000313|EMBL:ACI55299.1};
OS Rhizobium leguminosarum bv. trifolii (strain WSM2304).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=395492 {ECO:0000313|EMBL:ACI55299.1, ECO:0000313|Proteomes:UP000008330};
RN [1] {ECO:0000313|EMBL:ACI55299.1, ECO:0000313|Proteomes:UP000008330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM2304 {ECO:0000313|EMBL:ACI55299.1,
RC ECO:0000313|Proteomes:UP000008330};
RX PubMed=21304679; DOI=10.4056/sigs.44642;
RA Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA Yates R., Howieson J.;
RT "Complete genome sequence of Rhizobium leguminosarum bv trifolii strain
RT WSM2304, an effective microsymbiont of the South American clover Trifolium
RT polymorphum.";
RL Stand. Genomic Sci. 2:66-76(2010).
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; CP001191; ACI55299.1; -; Genomic_DNA.
DR RefSeq; WP_012557872.1; NC_011369.1.
DR AlphaFoldDB; B5ZRL8; -.
DR STRING; 395492.Rleg2_2015; -.
DR KEGG; rlt:Rleg2_2015; -.
DR eggNOG; COG2989; Bacteria.
DR HOGENOM; CLU_020360_2_0_5; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000008330; Chromosome.
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 Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..636
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002841731"
FT DOMAIN 141..281
FT /note="L,D-transpeptidase scaffold"
FT /evidence="ECO:0000259|Pfam:PF20142"
FT DOMAIN 342..375
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 405..566
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 636 AA; 68617 MW; 5CD2E8A13496DBF7 CRC64;
MTFVLKSAAS ALAISCGVAA MSAAPAHAYT LMDMLRGDKQ RTQSTIFMDQ APGRPVPRGA
VGGSLGGLDP EAPLPKVSGP RYYTYKAETL QFVDTGKFAD PVVTGAVADV SASGDASAEP
AVQRRFLAQA KVRANADVAK VLEAYYGDSR NPLVWVDGNQ INDRAKSAMA TLADAASVGL
DPADYAVQAP AIDPANPDPT FRDRALTQFE LELSAKVLAF VQDTVRGRID PNKISGYHDF
QRKAVNLTSV LKLARMSPDV GAYIASRSPD GAQFEALKAE LAKLRAVDGG NEERIVVSLD
KSLKPGDSSP EIANIVKAIG KHGSETLKTD HAATLAAYAG STDYSPDIVS LVEAFQQERG
LKADGVIGQA TVRAMTGGDT NASKIDKLVV AMEQARWLPE DLGSRYVMIN QPAFMVYYHN
DGKEQLSMRV VVGGKNNQTY FFDDEIETVE FNPFWGVPQS IIINEMLPKL RSDPNYLDQL
GYEVEVNGHA VASSSVDWYG STNNVSVRQP PSSDNALGEL KILFPNSHAI YMHDTPSKSF
FKRDMRALSH GCVRLANPRA MAAAVLGTTV DDVAKQIATG QNHAVKVPQK IPVYVSYFTA
WPNKDGVVEY FDDVYGRDGY VDKAFDATTK ARGAQI
//