ID A0A1I3CIQ4_9RHOB Unreviewed; 479 AA.
AC A0A1I3CIQ4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Lipoprotein-anchoring transpeptidase ErfK/SrfK {ECO:0000313|EMBL:SFH74308.1};
GN ORFNames=SAMN04488021_13123 {ECO:0000313|EMBL:SFH74308.1};
OS Paracoccus aminovorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=34004 {ECO:0000313|EMBL:SFH74308.1, ECO:0000313|Proteomes:UP000183635};
RN [1] {ECO:0000313|EMBL:SFH74308.1, ECO:0000313|Proteomes:UP000183635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8537 {ECO:0000313|EMBL:SFH74308.1,
RC ECO:0000313|Proteomes:UP000183635};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOPU01000031; SFH74308.1; -; Genomic_DNA.
DR RefSeq; WP_074969456.1; NZ_LN832559.1.
DR AlphaFoldDB; A0A1I3CIQ4; -.
DR STRING; 34004.SAMN04488021_13123; -.
DR OrthoDB; 9787225at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000183635; 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:SFH74308.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000183635};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..479
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010304136"
FT DOMAIN 75..126
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 215..345
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 426..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 479 AA; 49913 MW; 30F562298B342C9C CRC64;
MFPISTTRGL LARLALASAA LFLPLAPAGA EIAPDPAAAV APPKPRALIS ITRDEIEAAQ
YDGSDLPPGQ SALTAKVQIL LDRSGISPGV VDGWRGGMSE SAIKAFQRRA GLPMSGRMDH
AVWDLLQGYA AAPLTADYTI TDEDATGLVD NIPADYAEKA AMRSQGYTSV LEKLAERFHM
DEKFLAKLNP GSGFRPGETI HVTVPAKPIR AAVTRIIVDK ATRRVAAYDA KGNMVADYPA
TVGSADTPSP HGKHLVDAVA LNPTYTYNPQ RNFKQGKNDR VLIVPPGPNG PVGNVWIDLS
EPSYGIHGTA TPSQLFLNQS HGCVRLTNWD AWELAHMVKA KVTTVEFLDP GTSIADVTGV
TPAAAAGRTA MATTLAPTRP PARGVRQPPV LAAAEPAPVP AEAAMTETVA ASTAAAVANP
GPLVITPETP ASAEPLVPQA APPAAVPEEP EYPSDVGLPD TLPGDPAGSV TLYPQPGQP
//
