ID D8MTH4_ERWBE Unreviewed; 902 AA.
AC D8MTH4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Cation-transporting P-type ATPase {ECO:0000313|EMBL:CAX60131.1};
GN Name=mgtA {ECO:0000313|EMBL:CAX60131.1};
GN OrderedLocusNames=EbC_26000 {ECO:0000313|EMBL:CAX60131.1};
OS Erwinia billingiae (strain Eb661).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=634500 {ECO:0000313|Proteomes:UP000008793};
RN [1] {ECO:0000313|EMBL:CAX60131.1, ECO:0000313|Proteomes:UP000008793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eb661 {ECO:0000313|EMBL:CAX60131.1,
RC ECO:0000313|Proteomes:UP000008793};
RX PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA Knaust F., Geider K., Reinhardt R.;
RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT tasmaniensis with the pear pathogen E. pyrifoliae.";
RL BMC Genomics 11:393-393(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FP236843; CAX60131.1; -; Genomic_DNA.
DR AlphaFoldDB; D8MTH4; -.
DR STRING; 634500.EbC_26000; -.
DR KEGG; ebi:EbC_26000; -.
DR eggNOG; COG0474; Bacteria.
DR HOGENOM; CLU_002360_9_0_6; -.
DR Proteomes; UP000008793; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR CDD; cd02080; P-type_ATPase_cation; 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; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF29; SECRETORY PATHWAY CALCIUM ATPASE, ISOFORM G; 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; SFLDG00002; C1.7:_P-type_atpase_like; 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 SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008793};
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 69..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 291..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 704..728
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 734..755
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 776..794
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 806..825
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 845..864
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 876..893
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..93
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 902 AA; 98082 MW; 0E4F3723A65EB358 CRC64;
MTKLATENKN FPPTPAADIP YYQLSAEQGL QRQHSSRNGL SQAEVNARQH QYGPNALPQT
KGKPAWLRFL AHFNDVLIYI LLAAALLTAV MGHWVDTLVI LGVAVINALI GHIQENNAEK
SLKSISNMLA SEAVVVRDGQ HSTQPTRDLV PGDIVILRAG DRIPADLRVI EAHNLRVEEA
ILTGESVSVS KTAEPLSGEL ALGDRTNLLF SGTTLSAGSG SGVVIATGGD TELGHINQMI
SGIEKHRTPL LVQIDKLGKA IFVIILLMMV ALFIFSLLWR DIPLDELLLS LISLAVAAVP
EGLPAIISII LSLGIQTMAR KHAIIRKLPI VETLGAMTVV CSDKTGTLTM NEMTVKAVIT
ADACYQVEGD SYEPVGNISL EGESTPLNIA PGSVLEDYLR TIDLCNDSQL MKDEQGHWTV
TGGPTEGALK VLAAKSGLPA IQVELKGKIP FDSQYKYMAT HHQVGDRNKI LVTGAPDVLF
ALARQQQSAH GLCAFDQAYW EEKITHYARQ GLRMVAAAWM PAPDDLTQLD HDVLHGGLIF
LGIAGMMDPP RPEAIYAIRT CQQAGVRVKM ITGDHPQTAM NIAQMLGMAN SDRALTGHDL
EAMNDEELRE AAVSYDIFAR TSPEHKLRLV KALQDKGEIV GMTGDGVNDA PALKQADVGI
AMGIKGTEVT KEAADMVLTD DNFATIAGAV QEGRRVYDNL KKTILFIMPT NLAQGLLIII
ALLAGNIVPL TPVLILWMNM ATSATLSFAL AFEAAERNVM LRPPRNPTQH VMDGFAIWRV
AFVGTLIALS AFALEAWLQP RGHSPEFIRT VLLQTLVTAQ WFYMLNCRVS NGFSLGRSVL
ANKGLWLVSG VLLLLQLMII YVPFMQLLFG TEAIPLRYWG ITLAIGAVLF LIVELEKKLM
RR
//
