ID A0A368YS22_9RHOB Unreviewed; 500 AA.
AC A0A368YS22;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Lipoprotein-anchoring transpeptidase ErfK/SrfK {ECO:0000313|EMBL:RCW82066.1};
GN ORFNames=DFP89_11325 {ECO:0000313|EMBL:RCW82066.1};
OS Paracoccus lutimaris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1490030 {ECO:0000313|EMBL:RCW82066.1, ECO:0000313|Proteomes:UP000253345};
RN [1] {ECO:0000313|EMBL:RCW82066.1, ECO:0000313|Proteomes:UP000253345}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8525 {ECO:0000313|EMBL:RCW82066.1,
RC ECO:0000313|Proteomes:UP000253345};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUL-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}.
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:RCW82066.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QPJL01000013; RCW82066.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368YS22; -.
DR OrthoDB; 9787225at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000253345; 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; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR InterPro; IPR038063; Transpep_catalytic_dom.
DR PANTHER; PTHR30582:SF30; BLR4375 PROTEIN; 1.
DR PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR Pfam; PF01471; PG_binding_1; 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 Lipoprotein {ECO:0000313|EMBL:RCW82066.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000253345};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..500
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016992275"
FT DOMAIN 76..127
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 216..346
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 381..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 500 AA; 51388 MW; DEE4E96BA0BF9DDA CRC64;
MLPTVTAAGA ASRLSLATVA LFLSLAPAWP QADSTATTST AAASVARAPA VITPAQIEAA
TYGGGDLPAG QSALTAKVQV LLDRSGISPG VVDGWRGGMS ESAVKAFQRR AGLPMTGRMD
HAVWDLLQAY AAAPVTMAYT ITEDDAYGLV DQIPADYAEK AKMSSQGYTS ILEKLSERFH
MDEKFMIKLN PGVEFLPGAI IQATVPAKPI RATVTRIIVD KETRRVAAYD GRGNLVADYP
ATVGSTETPS PHGNHVVDAV ALNPTYTYNP KRNFKQGEND RVLIVPAGPN APVGNVWIDL
SEPTYGIHGT ATPSKLFVSQ SHGCVRLTNW DAWELAHMVK AKQTTVEFLD PGVSIADVTG
ASPAAAATRT TAVTAISATR PLARGNRVPP QLAGAAPIPA AQPAAQPTAQ STVLPAAAAP
AATPPVDALA ASLAKAGAEV APAAVITPAT PASSEPLAPA HAAPAAMTDE PEYPSDAGLP
GSLPDQQVGV VTLPPQGGQP
//
