ID S9RLT1_9RHOB Unreviewed; 536 AA.
AC S9RLT1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=L,D-transpeptidase YcbB {ECO:0000313|EMBL:EPX79060.1};
GN ORFNames=thalar_01877 {ECO:0000313|EMBL:EPX79060.1};
OS Litoreibacter arenae DSM 19593.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Litoreibacter.
OX NCBI_TaxID=1123360 {ECO:0000313|EMBL:EPX79060.1, ECO:0000313|Proteomes:UP000015351};
RN [1] {ECO:0000313|Proteomes:UP000015351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19593 {ECO:0000313|Proteomes:UP000015351};
RX PubMed=24501650; DOI=10.4056/sigs.4258318;
RA Riedel T., Fiebig A., Petersen J., Gronow S., Kyrpides N.C., Goker M.,
RA Klenk H.P.;
RT "Genome sequence of the Litoreibacter arenae type strain (DSM 19593(T)), a
RT member of the Roseobacter clade isolated from sea sand.";
RL Stand. Genomic Sci. 9:117-127(2013).
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:EPX79060.1}.
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DR EMBL; AONI01000010; EPX79060.1; -; Genomic_DNA.
DR RefSeq; WP_021100440.1; NZ_KE557306.1.
DR AlphaFoldDB; S9RLT1; -.
DR STRING; 1123360.thalar_01877; -.
DR PATRIC; fig|1123360.3.peg.1860; -.
DR eggNOG; COG2989; Bacteria.
DR HOGENOM; CLU_020360_3_4_5; -.
DR OrthoDB; 9778545at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000015351; 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; IPR006311; TAT_signal.
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; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000015351};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..536
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004555798"
FT DOMAIN 52..185
FT /note="L,D-transpeptidase scaffold"
FT /evidence="ECO:0000259|Pfam:PF20142"
FT DOMAIN 213..267
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 296..452
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 536 AA; 60012 MW; D977BC8642F61265 CRC64;
MTLSPTRRST LKLIAAGVAG AMLPSFGAGR ADAAVTALKQ SIAEAAARDE GLSTFYRKRN
YKPVFVGKGD SRRCAALLRA LERAGDHGLP VGAYDADGLK AAMKDARTPS DMGRVEVEAA
KRMLDFADHM RSGVLDPRSV DNMLVMDVPR YDRASTIDAF AKSNPAAFLR KMAPRKPEYV
RLQKEKLKLE KLLARGGWGD KVQAKTLKPG ETGGAVIQLR NRLIRMGYLR KSASQTYDAK
MQAAVQSFQV NHGLAPDGVA GGSTIAQINQ DVQDRLQQVL VAMERQRWNS RPMEKHHIWV
NIPDFHVDII KNGKSTFRSR VVVGKNTSDR RTPEFSDKME FMVVNPSWYV PRSIVTKEYL
PLMQRNRGAA RQLQIIGRNG RPVNRANINF AQYNARNFPY SMKQPPSKGN ALGLVKFMFP
NKHNIYLHDT PSKSLFGQEM RAFSHGCIRV HKPFDFAYAL LANQESNPEG FFQNVLRTGQ
ERRVDLREPM PVHIAYYTAW VDAKGQAHYR NDVYNRDSRI FDALSRAGVS LGSVAS
//