ID A0A1I5N233_9SPHN Unreviewed; 403 AA.
AC A0A1I5N233;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Putative peptidoglycan binding domain-containing protein {ECO:0000313|EMBL:SFP15682.1};
GN ORFNames=SAMN04488060_1724 {ECO:0000313|EMBL:SFP15682.1};
OS Qipengyuania nanhaisediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Qipengyuania.
OX NCBI_TaxID=604088 {ECO:0000313|EMBL:SFP15682.1, ECO:0000313|Proteomes:UP000199331};
RN [1] {ECO:0000313|Proteomes:UP000199331}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7715 {ECO:0000313|Proteomes:UP000199331};
RA Varghese N., Submissions S.;
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; FOWZ01000002; SFP15682.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5N233; -.
DR STRING; 604088.SAMN04488060_1724; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000199331; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..403
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012904549"
FT DOMAIN 79..132
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 273..400
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 21..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 403 AA; 43248 MW; 7008E9AB214E3299 CRC64;
MRQFLFIAAS SLALAACGMD GAEDDTDTNT ASAETRSAPD QGYETYSDDN YADSMASNDD
ASDTSGNSDA QIEDPEDRPV MQAQVVLDRI GFGPGVIDGK MGMSTENALT GFQEANDLEV
TGKLDEKTKS ALAEWDRIPA TRVVTIPASW GDIEFKEIPE DTAKKAEMEN LGYTSLDEKL
AERFHTTVEV LRQLNPNGRP AGASDTDQSN TNDAEADAPP TKRPGDGYFR AGQQIRVPNI
GGDAIEPGAI TDKGWQQTLA ALGVGSDQPE VDRIVVSKSE DTLKAYQGDK LVAMFTVSSG
SSQFPLPIGE WDILGEAYNP PYSYDPEVLG EGEGETFQLP PGPNGPVGVV WIDLSKEHYG
IHGTPEPETI GRAQSSGCVR LTNWDAARLA RMVSPSTQVI FEA
//
