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Database: UniProt
Entry: A0A0L7TBK7_9GAMM
LinkDB: A0A0L7TBK7_9GAMM
Original site: A0A0L7TBK7_9GAMM 
ID   A0A0L7TBK7_9GAMM        Unreviewed;       591 AA.
AC   A0A0L7TBK7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Peptidase {ECO:0000313|EMBL:KOC92747.1};
GN   ORFNames=NG42_00090 {ECO:0000313|EMBL:KOC92747.1}, NG43_01085
GN   {ECO:0000313|EMBL:KOC95332.1};
OS   Winslowiella iniecta.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Winslowiella.
OX   NCBI_TaxID=1560201 {ECO:0000313|EMBL:KOC92747.1, ECO:0000313|Proteomes:UP000037088};
RN   [1] {ECO:0000313|Proteomes:UP000036851, ECO:0000313|Proteomes:UP000037088}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B120 {ECO:0000313|EMBL:KOC92747.1,
RC   ECO:0000313|Proteomes:UP000037088}, and B149
RC   {ECO:0000313|EMBL:KOC95332.1, ECO:0000313|Proteomes:UP000036851};
RX   PubMed=26198254;
RA   Campillo T., Luna E., Portier P., Fischer-Le Saux M., Lapitan N.,
RA   Tisserat N.A., Leach J.E.;
RT   "Erwinia iniecta sp. nov., isolated from Russian wheat aphids (Diuraphis
RT   noxia).";
RL   Int. J. Syst. Evol. Microbiol. 0:0-0(2015).
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:KOC92747.1}.
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DR   EMBL; JRXE01000001; KOC92747.1; -; Genomic_DNA.
DR   EMBL; JRXF01000001; KOC95332.1; -; Genomic_DNA.
DR   RefSeq; WP_052896520.1; NZ_JRXF01000001.1.
DR   AlphaFoldDB; A0A0L7TBK7; -.
DR   STRING; 1560201.NG42_00090; -.
DR   PATRIC; fig|1560201.3.peg.21; -.
DR   OrthoDB; 9778545at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000036851; Unassembled WGS sequence.
DR   Proteomes; UP000037088; Unassembled WGS sequence.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProt.
DR   GO; GO:0016757; F:glycosyltransferase 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; L,D-TRANSPEPTIDASE HI_1667-RELATED; 1.
DR   PANTHER; PTHR41533:SF1; L,D-TRANSPEPTIDASE YCBB-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:UP000037088};
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..591
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008219488"
FT   DOMAIN          69..200
FT                   /note="L,D-transpeptidase scaffold"
FT                   /evidence="ECO:0000259|Pfam:PF20142"
FT   DOMAIN          290..323
FT                   /note="Peptidoglycan binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF01471"
FT   DOMAIN          351..518
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
SQ   SEQUENCE   591 AA;  65372 MW;  9CAB2D5AB3688663 CRC64;
     MLLANRVNLK KASLGCCIVL CLAQVYSATA AINSPLPASS ASSIMTAAQS QSQILAALPH
     SVKPFYLGSL ASLYAARDMQ PLWQDREAVQ QFQQQLAEVA ISGVQPQFTQ WIQQLTDPEI
     TGLARDIILS DAMLGYLQFV SSVPVQGEKW LYSNVPYKMT LPPVSVINQW QTAADAGGLN
     TFVVSLAPQH PQYTRMHQAL KTMLADNRPW PQLRDKQTLR PGQISQDVPA LREILQRTGM
     LSDNAEPPQP VDQAAVAVSP SATNVADLPV NTPEQSSNLL PQATSTTSAN IYSPELVEGL
     KRFQQWQGLA SDGAIGPRTR EWLNVSPQLR ASLLALNIQR LRLLPDDMHN GIMVNIPNYS
     LIYYSEGNEI LSSRVIVGRP DRKTPLMRSA LNNVVLNPPW NVPTSLVRQD IIPKVKRDPS
     YLYKHGYTLL SGWSNDAEVI DPSMIDWSMV SAASFPYRLR QAPGSANSLG RYKFNMPSSD
     AIYLHDTPNH NLFQKDIRAL SSGCVRVNKA SDLANLLLQD AGWNDSRISS TLKEGNTRFV
     SIRHRIPVNL YYLTAWVADD GKPQFRTDIY NYDATARSGS QVLARAGQLL L
//
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