ID A0A1M7P740_9BACT Unreviewed; 940 AA.
AC A0A1M7P740;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=ATPase, P-type (Transporting), HAD superfamily, subfamily IC {ECO:0000313|EMBL:SHN11978.1};
GN ORFNames=SAMN04488057_10747 {ECO:0000313|EMBL:SHN11978.1};
OS Cyclobacterium lianum.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Cyclobacterium.
OX NCBI_TaxID=388280 {ECO:0000313|EMBL:SHN11978.1, ECO:0000313|Proteomes:UP000184513};
RN [1] {ECO:0000313|EMBL:SHN11978.1, ECO:0000313|Proteomes:UP000184513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6102 {ECO:0000313|EMBL:SHN11978.1,
RC ECO:0000313|Proteomes:UP000184513};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FRCY01000007; SHN11978.1; -; Genomic_DNA.
DR RefSeq; WP_073094967.1; NZ_FRCY01000007.1.
DR AlphaFoldDB; A0A1M7P740; -.
DR STRING; 388280.SAMN04488057_10747; -.
DR OrthoDB; 1521937at2; -.
DR Proteomes; UP000184513; 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; 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; 2.
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 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 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 Reference proteome {ECO:0000313|Proteomes:UP000184513};
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 68..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 259..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 700..720
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 732..751
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 772..795
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 801..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..891
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 19..92
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 940 AA; 103187 MW; 1F571C4A25A50E75 CRC64;
MKTKDTKNKK SSNSTGQVHW HSLPVDEIYR RLDTSPEGLT DKSAEERSLK YGWNKLPEKS
GVNPVMKFLK HFDNLLIYIL LIAAVITALM GNWLVTGVIF GVELINAVIG YIQENKAERA
IRGISNMLPG HAKVIRSSQT KSILAESLVP GDIVLLKAGD KIPADIRLTE ATNMKIEEAV
LTGESLPVNK TTEVFPEESL PADRKCMAYS GTLVTNGIGT GIVVCTGVHT QIGQISKMME
DVQTLSTPLM RKFDRFGKML AIAIIFLSAI FFMLGYFIQG YALNELFLIV VGIAVSLIPE
GLPVLMTITL AKGVLKMAKQ NAIIRKLPSV ETLGEVTVIC SDKTGTLTKN EMTVTDVLLA
NKQYTVTGVG YSPVGEIFDN GKKVAMGESD GFDELLQGVA LCSNSEANKS GDEWSIIGDP
TESALLSLAL KGGYYGFKNN KRLDIIPFDS SQKFMAVLIP GEHFNTIYLK GAPEKVLEMS
VFHGSIGQSD TNSPEWWKEQ LSSLASEGKR IIATASKKVP LDYKNILLSD VFNMDFLGIV
AMIDPPRQEA IKAIEQCHQA GVEVKMITGD HTLTAKAIGE SLNIVKEDNV ISGPELEKLS
DIELEAVAKK YQVFARTTPE HKLRLVKALQ SNGQIVAMTG DGVNDAPALK RADVGIAMGI
KGTDVTKDSA EMILADDNFA TIAKAVFEGR SIYDNLKKSI LFVLPTNGAE GFVMMASVLI
GGHMPITPLQ ILWINLVTAV TLGFALAFEP GEPNVTTRPP RKPNEPILDG FLIWRIGFVS
VLLGSITLMV HHFLIQFGAD YGHARSAAVN TLVAGEVFYL LNCRYLREPV LGKGFFSNPK
VFYAISSVVL IQLFFTYTPF MNILFDTTPL HTRELTWILA AGLLFFIIVE IEKMITKKIF
DNDSEKGGYF NPFKKIVPIR KSENGTMKSL WSNPSRNNFM
//
