ID A0A0W0YLB0_9GAMM Unreviewed; 379 AA.
AC A0A0W0YLB0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=UDP-N-acetylmuramyl tripeptide synthase {ECO:0000313|EMBL:KTD57611.1};
GN ORFNames=Lsha_2452 {ECO:0000313|EMBL:KTD57611.1};
OS Legionella shakespearei DSM 23087.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1122169 {ECO:0000313|EMBL:KTD57611.1, ECO:0000313|Proteomes:UP000054600};
RN [1] {ECO:0000313|EMBL:KTD57611.1, ECO:0000313|Proteomes:UP000054600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49655 {ECO:0000313|EMBL:KTD57611.1,
RC ECO:0000313|Proteomes:UP000054600};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KTD57611.1}.
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DR EMBL; LNYW01000066; KTD57611.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0YLB0; -.
DR STRING; 1122169.Lsha_2452; -.
DR PATRIC; fig|1122169.6.peg.2819; -.
DR eggNOG; COG0189; Bacteria.
DR Proteomes; UP000054600; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR PANTHER; PTHR21621:SF0; BETA-CITRYLGLUTAMATE SYNTHASE B-RELATED; 1.
DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR Pfam; PF08443; RimK; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000054600};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 355..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 81..336
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 379 AA; 43334 MW; A6BA6CA55DD97E85 CRC64;
MLYYQTRLSS IRFSFWRRII NTDAALYYKR AKALLLPVEP KPEVYGFELK ISNRHYLFYN
NDTPFNNSSS SFIAINKYCT NQILAAANIP VPKGILFHTT DLEHDSLENI IANLRFPLVI
KPADGSLGMG VLCNIKTFDE LSFFLKQYCS VYPSMIIEEF YGNLQSYRVL VFNRKIIGVV
LCQPARVLGD GKHTIQELIE LTNTKRKEIS DSLDPIVLDD ECQLRLKELG IDQSYIPASG
ETIVLCYTSN PTRGGSYESV DLKICKENRK IITKAAKVLN LKLAGIDIEC TDINTPFSLS
QGVILDVNHR PSMLIHELPI NGKPQPVTKK IMKSFIFRHP FTYLYSLYSN RSTSFYMRAL
TVSLIAALIY WFAYQYFEG
//
