ID A0A1H3YLJ3_9GAMM Unreviewed; 572 AA.
AC A0A1H3YLJ3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Murein L,D-transpeptidase YcbB/YkuD {ECO:0000313|EMBL:SEA11904.1};
GN ORFNames=SAMN02982996_01022 {ECO:0000313|EMBL:SEA11904.1};
OS Lonsdalea quercina.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Lonsdalea.
OX NCBI_TaxID=71657 {ECO:0000313|EMBL:SEA11904.1, ECO:0000313|Proteomes:UP000187280};
RN [1] {ECO:0000313|EMBL:SEA11904.1, ECO:0000313|Proteomes:UP000187280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29281 {ECO:0000313|EMBL:SEA11904.1,
RC ECO:0000313|Proteomes:UP000187280};
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; FNQS01000002; SEA11904.1; -; Genomic_DNA.
DR RefSeq; WP_026742704.1; NZ_FNQS01000002.1.
DR AlphaFoldDB; A0A1H3YLJ3; -.
DR STRING; 71657.SAMN02982996_01022; -.
DR eggNOG; COG2989; Bacteria.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000187280; 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:UP000187280};
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..572
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010585728"
FT DOMAIN 70..201
FT /note="L,D-transpeptidase scaffold"
FT /evidence="ECO:0000259|Pfam:PF20142"
FT DOMAIN 268..304
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 332..499
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 572 AA; 62631 MW; A2D887BD5DD988CF CRC64;
MLLAKRKMQG LRLGITGGAL CLGGLIAFSA QAATQTMLSG TTTPISTAAP ATTGLAGPLP
AGITLHYGSA LRGLYTQTAE QPMWSDSRAV NAFQQQLAEL ALAGIQPQFT TWVSWLTDPK
LAGLARDRVL SDAMLGYLQY VSGVDKNGSN WLYANVPYTL SLPPSGLITE WQNAVKEGRS
AEFVASLAPR HSQYVKMHEA LKASLLDKRP WPKLQLGGTL RPGDQSSELP ALQEILQRTG
MLASNATTLP LFNESPSTDG SIASAPSGAT NVYTGELVDA VKRFQHWHGL QDDGAIGKRT
KDWLNVSSQT RATLLALNIQ RLRLIPDNVS NGILVNIPNF SLTYYQNGAE ILSSRVIVGQ
PKRKTPLMSS ALVNVVVNPP WNVPTTLTRQ DIIPKVIMDP GYLQRHGYTL LSDWSENAQP
IDPTMIDWSQ VSAERFPYRL RQAPGSTNSL GRYKFNMPNS EAIYLHDTPN HNLFHKDIRA
LSSGCVRVNK AAELAGLLLQ DAGWNSARVS STLEEGNTTY VTMRKRIPVN FYYLTAWVAE
DGKAQYRTDI YNYDGRSKTG ESMLSKVGLL LQ
//
