ID F4MQZ0_MYCML Unreviewed; 942 AA.
AC F4MQZ0;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Magnesium-transporting ATPase, P-type 1 {ECO:0000256|ARBA:ARBA00013555};
DE EC=7.2.2.14 {ECO:0000256|ARBA:ARBA00012786};
DE AltName: Full=Mg(2+) transport ATPase, P-type 1 {ECO:0000256|ARBA:ARBA00029806};
GN Name=mgtA {ECO:0000313|EMBL:CBW54524.1};
GN ORFNames=MLC_7940 {ECO:0000313|EMBL:CBW54524.1};
OS Mycoplasma mycoides subsp. capri LC str. 95010.
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=862259 {ECO:0000313|EMBL:CBW54524.1, ECO:0000313|Proteomes:UP000010103};
RN [1] {ECO:0000313|EMBL:CBW54524.1, ECO:0000313|Proteomes:UP000010103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=95010 {ECO:0000313|EMBL:CBW54524.1,
RC ECO:0000313|Proteomes:UP000010103};
RA Thiaucourt F., Manso-Silvan L., Salah W., Barbe V., Berger A., Jacob D.,
RA Breton M., Dupuy V., Lomenech A.M., Blanchard A., Sirand-Pugnet P.;
RT "Mycoplasma mycoides, from "mycoides Small Colony" to "capri". A
RT microevolutionary perspective.";
RL BMC Genomics 0:0-0(2011).
RN [2] {ECO:0000313|Proteomes:UP000010103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=95010 {ECO:0000313|Proteomes:UP000010103};
RX PubMed=21324191; DOI=10.1186/1471-2164-12-114;
RA Thiaucourt F., Manso-Silvan L., Salah W., Barbe V., Berger A., Jacob D.,
RA Breton M., Dupuy V., Lomenech A.M., Blanchard A., Sirand-Pugnet P.;
RT "Mycoplasma mycoides, from "mycoides Small Colony" to "capri". A
RT microevolutionary perspective.";
RL BMC Genomics 12:114-114(2011).
RN [3] {ECO:0000313|Proteomes:UP000010103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=95010 {ECO:0000313|Proteomes:UP000010103};
RA Thiaucourt F., Manso-Silvan L., Salah W., Barbe V., Berger A., Jacob D.,
RA Breton M., Dupuy V., Lomenech A.M., Blanchard A., Sirand-Pugnet P.;
RT "Mycoplasma mycoides, from mycoides Small Colony to capri. A
RT microevolutionary perspective.";
RL BMC Genomics 12:0-0(2011).
CC -!- FUNCTION: Mediates magnesium influx to the cytosol.
CC {ECO:0000256|ARBA:ARBA00003954}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + Mg(2+)(out) = ADP + H(+) + Mg(2+)(in) + phosphate;
CC Xref=Rhea:RHEA:10260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18420, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.14;
CC Evidence={ECO:0000256|ARBA:ARBA00001857};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIIB subfamily. {ECO:0000256|ARBA:ARBA00008746}.
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DR EMBL; FQ377874; CBW54524.1; -; Genomic_DNA.
DR RefSeq; WP_013729892.1; NC_015431.1.
DR AlphaFoldDB; F4MQZ0; -.
DR KEGG; mml:MLC_7940; -.
DR HOGENOM; CLU_002360_6_3_14; -.
DR OrthoDB; 9813266at2; -.
DR Proteomes; UP000010103; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0015444; F:P-type magnesium transporter activity; IEA:UniProtKB-EC.
DR CDD; cd02077; P-type_ATPase_Mg; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006415; P-type_ATPase_IIIB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01524; ATPase-IIIB_Mg; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF156; CALCIUM-TRANSPORTING ATPASE; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022519};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 79..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 306..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 793..821
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 841..863
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 875..897
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 909..930
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 31..103
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 942 AA; 105893 MW; D949B2CC927CFB88 CRC64;
MFLFKKRKFS PKKITRHKKK THFANERFIK QVSNLEQNEV LEIMQLQHFG LTNEQYESRL
KKYGTNELKK KRFNLIAEFL HAFFGPFNIV LLLISLYNFI SYATNGFYQD TNSSDSKFEL
VGALIILVMV LASGLASFIQ SLRSHLVTKK ISSIVKSTTN IIRHKNDEDV EDYLKITKRN
QLDLIRLGEE IDVKQLVPGD LIYLSSGDML PADVRIIQST DLFINQSSLT GESIPVEKHA
NNKKNTNNIL DLENICYTGT SVVSGSALAV VLATANDTYF STISKAILEK RPDSSFTKGI
KQVTRMLLIF MLVMVPTVYL AKSIIGTISS GGSFDSIKDN PWFQAIFFAV AVAVGLTPEM
LPMIVTTNLA NGASKMSKQK VVVKQLEAIQ SLGAIDVLCT DKTGTLTNDK IELVDYLRVD
KKADPTLLKY LYINSYYQTG LKNPMDKAIV DYVNKHNHNF SIQDITKIDE IPFDFNRRKL
TIIFDDENEK RFMVTKGSVE EILNSCTRVI QDDKIVNLTD TFKRQIIAYY ETINQQGKRL
LGVAYKKIRD NQAKFSPKDE ESLIFMGFAS FLDTPKPSTK QTIKLLKKYG VDLKILTGDS
EPITRAICKM VNLDIKGLVT GEEIDAASEY ELKKIVEDNN IFVKLNPLQK VKIIQVLKQN
NHVVGYMGDG INDAPVLRQS DVAISVNNAT EIAKDASDII LLEKSLLVLE KGIIQGRTIF
GNILKYIKIT TASNFGNALS VLIGTVWLPF SPMAPAQILL QNLIYDFSQF GVALDRVDST
FLTSPQRWQS KDLLPFTTIN GSISTIFDLI TFAIAGYYFG FITSYNSAIA QNNSLLAAQS
LAQFHACWFI IGLLSQTFVF QILRTEQLPV IQSRSTWPVY VIGALATIMA FSIVYISQIG
SLVQLQSPGL IYIPISIAII FSYCLIAQLT KVGYKKVFKR WL
//
