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Database: UniProt
Entry: A0A0Q6ZES7_9BRAD
LinkDB: A0A0Q6ZES7_9BRAD
Original site: A0A0Q6ZES7_9BRAD 
ID   A0A0Q6ZES7_9BRAD        Unreviewed;       704 AA.
AC   A0A0Q6ZES7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Peptidoglycan-binding protein {ECO:0000313|EMBL:KQW21901.1};
GN   ORFNames=ASC80_00350 {ECO:0000313|EMBL:KQW21901.1};
OS   Afipia sp. Root123D2.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Afipia.
OX   NCBI_TaxID=1736436 {ECO:0000313|EMBL:KQW21901.1, ECO:0000313|Proteomes:UP000051348};
RN   [1] {ECO:0000313|EMBL:KQW21901.1, ECO:0000313|Proteomes:UP000051348}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root123D2 {ECO:0000313|EMBL:KQW21901.1,
RC   ECO:0000313|Proteomes:UP000051348};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQW21901.1, ECO:0000313|Proteomes:UP000051348}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root123D2 {ECO:0000313|EMBL:KQW21901.1,
RC   ECO:0000313|Proteomes:UP000051348};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQW21901.1}.
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DR   EMBL; LMDP01000001; KQW21901.1; -; Genomic_DNA.
DR   RefSeq; WP_056291751.1; NZ_LMDP01000001.1.
DR   AlphaFoldDB; A0A0Q6ZES7; -.
DR   STRING; 1736436.ASC80_00350; -.
DR   OrthoDB; 9778545at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000051348; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000051348};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..704
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006299970"
FT   DOMAIN          173..306
FT                   /note="L,D-transpeptidase scaffold"
FT                   /evidence="ECO:0000259|Pfam:PF20142"
FT   DOMAIN          351..394
FT                   /note="Peptidoglycan binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF01471"
FT   DOMAIN          428..573
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
FT   REGION          51..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   704 AA;  76290 MW;  7F8CC1EF4FE58B12 CRC64;
     MRNYLNRRSG FDRTLAAIAA TFLSIGAASL AHADPAKTSA DLAIDAAVPM PEPANVPPPT
     AADFNPVAPV ASEAPKTTEA PKTTEAPKTA ETPAADTSKA PAATATAPSS APPANETATA
     PAAAPAATPS AAASPAEATS SIAAADQPFA DKLRDLVTTK SAKYFDRKAE RVAVEAFYKD
     RNYAPLWTAG SAPSAQANGA ISRLKDAASD GLDPADYPVP NFAAANTPEA QAEAELKITA
     SILDYARHAQ AGRMHWSQVS GDILYPEHNP EPAEVLVNVS TAKDASAALD SYNPPSRDYQ
     ALKAKLAELR GVTETPQHKF EDGATLRYVK PRKGSDAEPM DDPRVPALRA RLGITENPND
     THYDATVDAA VRKFQAQNGL KADGIVAQNT IRALNGERKD RKVDIVRVNM ERLRWLPRHL
     GAKSLGDAYV ILNIPDYSLK VMHNGKQAWK TRVVVGKVGK HATPLLTETM KYITVNPTWN
     VPPSIIYNEY LPALQQDPTV LDRMGLKMSR NSDGSIRISQ PPGEANALGR IRFNFPNKFL
     VYQHDTPDKN LFAKETRAYS HGCMRVQNPD QYAATLLGIA LPKENYTPEK IRSMYGRGEV
     NINLPTPIPV NIVYQTAFVD DAGKLEFRND IYGRDAKMIS LLNGSGKNLE TVIAHSQPTY
     TRPTNVRVPG ESFADSSGPN LFEMLFGGGR PQREEPQTRR RVYR
//
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