ID D5Q4P3_CLODI Unreviewed; 886 AA.
AC D5Q4P3;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Putative potassium/sodium efflux P-type ATPase, fungal-type {ECO:0000313|EMBL:EFH07099.1};
GN ORFNames=HMPREF0220_1875 {ECO:0000313|EMBL:EFH07099.1};
OS Clostridioides difficile NAP08.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=525259 {ECO:0000313|EMBL:EFH07099.1, ECO:0000313|Proteomes:UP000003227};
RN [1] {ECO:0000313|EMBL:EFH07099.1, ECO:0000313|Proteomes:UP000003227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAP08 {ECO:0000313|EMBL:EFH07099.1,
RC ECO:0000313|Proteomes:UP000003227};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFH07099.1}.
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DR EMBL; ADNX01000043; EFH07099.1; -; Genomic_DNA.
DR RefSeq; WP_003423887.1; NZ_GG770710.1.
DR AlphaFoldDB; D5Q4P3; -.
DR HOGENOM; CLU_002360_3_0_9; -.
DR Proteomes; UP000003227; Unassembled WGS sequence.
DR GO; GO:0016020; C: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 CDD; cd02089; P-type_ATPase_Ca_prok; 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; PTHR43294:SF22; P-TYPE ATPASE; 1.
DR PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 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 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 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 56..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 85..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 275..303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 684..705
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 711..733
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 824..844
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 856..874
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..81
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 886 AA; 97218 MW; 7C0A9F7833BA1E8F CRC64;
MENHKQMPWH SRATHEILES LDSSEEGLTD TEAEKRLKEN GLNELRKKPN RTTLQMLWSQ
ITDAMVLILI GAAILSLIFG EFTEAFVILI IVTVNAVIGI VQEKKAESSL EALKNMNSPT
ARVMRDGEEN VIPASNLVVG DIVFLEDGAM VPADLRLIET SSLKIQEASL TGESVPSEKD
ADTILPKEYV LGDRSNMAYT SSIVTYGRGV GVVVATGMNT EVGNIAHLLD SQDDFDTPIK
RKLNTVGKTL SVIGIIVCVV IFAIGAFYQR PLLPMFMIAI SLAISIIPEG LPATATIVMA
LGVQRMSKRN ALIRKLPAVE TLGGATVICC DKTGTLTLNK MTVTHIAVNG DFESGKVTSI
DTASEKHPLV YKEIVYAGAL CNDACINPDK TDEILGDPTE GALIFMAKKF GIDQEILEEE
YPRVFEQPFD SDRKCMTTVH NIDEKIIAYT KGAVDEILDL CTKILTSKGE RNITELDKKN
IHELCLNMSK DALRVLGFAK REISSIPKED SENIEYDLTF IGIVGMIDPP RTEVIDAVST
CKEAGIRTIM ITGDHKVTAT TIAHELGIWS EENTVISGDE LDNLSDDELD EAVKNTTVFA
RVSPFDKLRI IQSLKRIGEV PAMTGDGVND SPALKSADIG IAMGISGTDV AKDSSDMILM
DDSFTTISYA IKEGRRVYRN IQKVIQFLLV GNIAEILTLF VAILLNWDTP LLAVHILWVN
LATATLPALA LGVDPPSRNI MKHQPVKSTT LFEKNLIQRV VTQGIFVAIM TILAYKIGLN
IENHSVGQTM AFCVLAFSQM LRAFSQRSNT DSMFNRNNGK NPFLLISFLT SALLIAVILF
VPVFRNAFNL TILNSLEWLI TIALAIMSVV QVEVGKIIKR KKLKNS
//
