ID A6TUJ5_ALKMQ Unreviewed; 714 AA.
AC A6TUJ5;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=D-alanine--D-alanine ligase domain protein {ECO:0000313|EMBL:ABR49863.1};
GN OrderedLocusNames=Amet_3744 {ECO:0000313|EMBL:ABR49863.1};
OS Alkaliphilus metalliredigens (strain QYMF).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=293826 {ECO:0000313|EMBL:ABR49863.1, ECO:0000313|Proteomes:UP000001572};
RN [1] {ECO:0000313|Proteomes:UP000001572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QYMF {ECO:0000313|Proteomes:UP000001572};
RX PubMed=27811105; DOI=10.1128/genomeA.01226-16;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA Richardson P., Fields M.W.;
RT "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT leachate ponds.";
RL Genome Announc. 4:0-0(2016).
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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DR EMBL; CP000724; ABR49863.1; -; Genomic_DNA.
DR RefSeq; WP_012064823.1; NC_009633.1.
DR AlphaFoldDB; A6TUJ5; -.
DR STRING; 293826.Amet_3744; -.
DR KEGG; amt:Amet_3744; -.
DR eggNOG; COG0624; Bacteria.
DR eggNOG; COG1181; Bacteria.
DR HOGENOM; CLU_386694_0_0_9; -.
DR OrthoDB; 9813261at2; -.
DR Proteomes; UP000001572; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR011095; Dala_Dala_lig_C.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR PANTHER; PTHR23132:SF23; D-ALANINE--D-ALANINE LIGASE B; 1.
DR Pfam; PF07478; Dala_Dala_lig_C; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ABR49863.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000001572}.
FT DOMAIN 119..320
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 714 AA; 79750 MW; 990699D74A9C9D22 CRC64;
MKIAIVYNRE SQAVINLFGT LNREKYGLET INKIKEGLTA GGHQVKTFEG DKNIITKLEK
FMPSVISGER PGLVFNLSYG IQGKGRYMHV PGILEMLGIP YVGSGPETHA IALDKIVTKM
ILIQKGLPTP KFTVMDKPDS EIKDNLKYPL IVKPKDEAVS FGLKIVHNEE ELRDGVKTIY
EAFNTPTLVE EYIEGREINV GLLGNNPVEA MPPVELTFGE GLQIYTYEDK KNTSGRTVEK
ICPAPLSDEK TEQIKQLAID TFNALGCYDS ARVDFRLDQE GNPYILEVNS MASLGKSGSF
VYAAEKMGLD YVALVNRLID VTCERYFGPH FFMNTDQEVA NEASNLFGAI TSNRDKIEDE
LKVWTNLSSW TEDPVGLSMV LRKLEDRLKK LGLKVVEEHT NGRSAWTWAT KEGLKDGTLL
VVPLDIPGER TGFPIPFRTD QEWMYGEGIA SSRGGLVTLL SALSALKGIK ALSTKKVGVL
FYSDEGRGMR YSSPTLRQAA KQAKQVIVLQ PGFEGGNIVD QRRGTKKYSI VIEGEPLRVG
RRSNQIDVLT YFLQKTEKLK EISSPDQRLT VAIHDVHSER YSVLLPHRVR ATVYVTFLEE
KMARDAETQI KEVFKSNARG MKTYVEKLEE RPPLLRKKNN PIVKRLGELC EEWNIPFGIE
SSLLATAAGE VPSSVPVICG FGPASKGLYT PNEAIHRGEM IQRSFLLSML LLEE
//