(data stored in ACNUC7421 zone)

HOGENOM: LACDA_1_PE915

ID   LACDA_1_PE915                        STANDARD;      PRT;   752 AA.
AC   LACDA_1_PE915; Q1G9S2;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   SubName: Full=Cation transporting P-type ATPase (LACDA_1.PE915) (Probable
DE   Cd2+/Mg2+ transporter); .
GN   OrderedLocusNames=Ldb1301;
OS   LACTOBACILLUS DELBRUECKII SUBSP. BULGARICUS ATCC 11842.
OC   Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae; Lactobacillus.
OX   NCBI_TaxID=390333;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS LACDA_1.PE915.
CC       Lactobacillus delbrueckii subsp. bulgaricus ATCC 11842, complete genome
CC       NRRL Y-1140) chromosome F, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:Q1G9S2_LACDA
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       family.
CC   -!- GENE_FAMILY: HOG000160005 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q1G9S2; -.
DR   EMBL; CR954253; CAI98102.1; -; Genomic_DNA.
DR   RefSeq; YP_619168.1; NC_008054.1.
DR   ProteinModelPortal; Q1G9S2; -.
DR   STRING; Q1G9S2; -.
DR   GeneID; 4084685; -.
DR   GenomeReviews; CR954253_GR; Ldb1301.
DR   KEGG; ldb:Ldb1301; -.
DR   eggNOG; COG0474; -.
DR   OMA; ILECILG; -.
DR   ProtClustDB; CLSK912463; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015662; F:ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism; IEA:InterPDR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006812; P:cation transport; IEA:InterPro.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-dom.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023300; ATPase_P-typ_cyto_domA.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR023214; HAD-like_dom.
DR   Gene3D; G3DSA:2.70.150.10; ATPase_P-typ_cyto_domA; 2.
DR   Gene3D; G3DSA:1.20.1110.10; ATPase_P-typ_TM_dom; 2.
DR   Gene3D; G3DSA:3.40.50.1000; HAD-like_dom; 2.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   HOGENOMDNA; LACDA_1.PE915; -.
KW   ATP-binding; Complete proteome; Hydrolase; Nucleotide-binding;
KW   Phosphoprotein; Transmembrane.
SQ   SEQUENCE   752 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKVKGLTQAE ADLRLKKDGL NQVPEPEFSF WKEFAGKLWN LSAWILEAAL LLECALGKWI
     QSLFVLLMLL FAAYNGATQK KKSRKVLSSI SQQLTPVVAV LRDDRWQKID SKYLVVGDIV
     NLQKGDILAA DIDLLDGNLT LDESSITGEA KNVHKKAGAT AFAGTTVMDG EALGRVSATG
     TNSRSGQTIN LINTSAAPGH LQQLLTKIIY YLCLLDGVLT VILLIAAVIR GENILEMLPF
     LAMMFIASIP VAMPSTFTLS NSFEATRLSK EGVLTSDLTG IQDAANLNLL LLDKTGTITE
     NKTAVASFAN FSKLSDEEVL ALTSLAIDQR NQSVIDLALM DFLQEKKIPV KEAEAFTPFT
     SSQGYSEGRG EGHDVKLGSV KQFSKIDPAI SEQMAAVDLS LGRSVGILLD DRLAGIFITK
     DKVRADSKAA LAELVKRGIK PVMLTGDNQK TAASVAEEVG LTGKVISISD FKEGVKAEDL
     AGIADVLPED KLDMVKYFQK AGYIVGMTGD GVNDSPALKQ AEVGIAVSNA ADVAKKSSKM
     VLLDEGLSPI VKILDAGHRV YQRMTTWSLT KLARTAELTM LLTFSYLIFG YLPMALNAMV
     IYTIMNNMVT MMIGTDKTHI TYKPENWDMG KLAKIAFSLA GAWTIIGFAF VSALTKAGVN
     HDQVGTMVYV FLVMSAMMIV LITRTKRFFW QSAPSKPVAS VQIADILLTC LLALLGIAMP
     AIGIKELLTP LAVAFLAAIL IDLVYQPVMK NK
//

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