ID A2TJJ0_ENTFL Unreviewed; 268 AA.
AC A2TJJ0;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE SubName: Full=Vancomycin resistance protein A {ECO:0000313|EMBL:ABN05630.1};
DE Flags: Fragment;
GN Name=vanA {ECO:0000313|EMBL:ABN05630.1};
OS Enterococcus faecalis (Streptococcus faecalis).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1351 {ECO:0000313|EMBL:ABN05630.1};
RN [1] {ECO:0000313|EMBL:ABN05630.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A21 {ECO:0000313|EMBL:ABN05630.1};
RX PubMed=18187222; DOI=10.1016/j.ijfoodmicro.2007.11.063;
RA Chan Y.Y., Abd Nasir M.H., Yahaya M.A., Salleh N.M., Md Dan A.D.,
RA Musa A.M., Ravichandran M.;
RT "Low prevalence of vancomycin- and bifunctional aminoglycoside-resistant
RT enterococci isolated from poultry farms in Malaysia.";
RL Int. J. Food Microbiol. 122:221-226(2008).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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DR EMBL; EF206286; ABN05630.1; -; Genomic_DNA.
DR AlphaFoldDB; A2TJJ0; -.
DR SMR; A2TJJ0; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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 InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR000291; D-Ala_lig_Van_CS.
DR InterPro; IPR005905; D_ala_D_ala.
DR InterPro; IPR011095; Dala_Dala_lig_C.
DR InterPro; IPR011127; Dala_Dala_lig_N.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR PANTHER; PTHR23132:SF25; D-ALANINE--D-ALANINE LIGASE A; 1.
DR Pfam; PF07478; Dala_Dala_lig_C; 1.
DR Pfam; PF01820; Dala_Dala_lig_N; 1.
DR PIRSF; PIRSF039102; Ddl/VanB; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00843; DALA_DALA_LIGASE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT DOMAIN 115..268
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABN05630.1"
FT NON_TER 268
FT /evidence="ECO:0000313|EMBL:ABN05630.1"
SQ SEQUENCE 268 AA; 29181 MW; B63373D6EFB3AE75 CRC64;
SAIEIAANIN KEKYEPLYIG ITKSGVWKMC EKPCAEWEND NCYSAVLSPD KKMHGLLVKK
NHEYEINHVD VAFSALHGKS GEDGSIQGLF ELSGIPFVGC DIQSSAICMD KSLTYIVAKN
AGIATPAFWV INKDDRPVAA TFTYPVFVKP ARSGSSFGVK KVNSADELDY AIESARQYDS
KILIEQAVSG CEVGCAVLGN SAALVVGEVD QIRLQYGIFR IHQEVEPEKG SENAVITVPA
DLSAEERGRI QETAKKIYKA LGCRGLAR
//
