ID A0A097EE95_9SPHN Unreviewed; 344 AA.
AC A0A097EE95;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 02-APR-2025, entry version 31.
DE SubName: Full=ErfK/YbiS/YcfS/YnhG {ECO:0000313|EMBL:AIT05884.1};
GN ORFNames=MC45_05075 {ECO:0000313|EMBL:AIT05884.1};
OS Sphingomonas taxi.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Sphingomonadales; Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1549858 {ECO:0000313|EMBL:AIT05884.1, ECO:0000313|Proteomes:UP000033200};
RN [1] {ECO:0000313|EMBL:AIT05884.1, ECO:0000313|Proteomes:UP000033200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55669 {ECO:0000313|EMBL:AIT05884.1,
RC ECO:0000313|Proteomes:UP000033200};
RA Zhou Y., Ma T., Liu T.;
RT "Using Illumina technology Improving SMRT sequencing Genome Assembly by
RT RASTools.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|PROSITE-ProRule:PRU01373}.
CC -!- SIMILARITY: Belongs to the YkuD family.
CC {ECO:0000256|ARBA:ARBA00005992}.
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DR EMBL; CP009571; AIT05884.1; -; Genomic_DNA.
DR RefSeq; WP_038660342.1; NZ_CP009571.1.
DR AlphaFoldDB; A0A097EE95; -.
DR STRING; 1549858.MC45_05075; -.
DR KEGG; stax:MC45_05075; -.
DR eggNOG; COG1376; Bacteria.
DR eggNOG; COG3409; Bacteria.
DR HOGENOM; CLU_042399_6_0_5; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000033200; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:TreeGrafter.
DR GO; GO:0071972; F:peptidoglycan L,D-transpeptidase activity; IEA:TreeGrafter.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-UniRule.
DR GO; GO:0018104; P:peptidoglycan-protein cross-linking; IEA:TreeGrafter.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-UniRule.
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; IPR050979; LD-transpeptidase.
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; PS52029; LD_TPASE; 1.
PE 3: Inferred from homology;
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|PROSITE-
KW ProRule:PRU01373};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|PROSITE-ProRule:PRU01373};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984,
KW ECO:0000256|PROSITE-ProRule:PRU01373};
KW Reference proteome {ECO:0000313|Proteomes:UP000033200};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..344
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001929827"
FT DOMAIN 210..343
FT /note="L,D-TPase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS52029"
FT ACT_SITE 303
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01373"
FT ACT_SITE 319
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01373"
SQ SEQUENCE 344 AA; 37321 MW; DE470DAB47457E79 CRC64;
MKMVLATALL AGAALAAPTI AQRTVAQPVP QAVPQPAAPA LDRNILHVQV ILDSLGFGPG
VLDGKGGQSL TAALKGFQEA KGLPRTGKPD AATLQALYPY RAKRPTARFV LTREALAGPY
YNPLPKDYGE QAKLPSLGYA TPMEKLAEMF HTQPAVLIAL NSPDTRLKVG NTIVVPNALP
ASRAYDPKLP DHWRQTLNML NVDANQPVAD HIVVDKSEKV LRVLDKDDKL IAQFSATMGS
EHDPLPLGTW KIYGADYNPK FHYNPALFWD AKKGDQKEML PPGPNGPVGV VWLDLSKEHY
GIHGTPHPEL IGRTESHGCI RLTNWDVARL AQMVKPGTKA VFQA
//
