ID A0A167WBW7_9FLAO Unreviewed; 864 AA.
AC A0A167WBW7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=ATPase {ECO:0000313|EMBL:OAB27211.1};
GN ORFNames=FBFR_11775 {ECO:0000313|EMBL:OAB27211.1};
OS Flavobacterium fryxellicola.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=249352 {ECO:0000313|EMBL:OAB27211.1, ECO:0000313|Proteomes:UP000077164};
RN [1] {ECO:0000313|EMBL:OAB27211.1, ECO:0000313|Proteomes:UP000077164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16209 {ECO:0000313|EMBL:OAB27211.1,
RC ECO:0000313|Proteomes:UP000077164};
RA Shin S.-K., Yi H.;
RT "Draft genome sequence of Flavobacterium fryxellicola DSM 16209.";
RL Submitted (MAR-2016) 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:OAB27211.1}.
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DR EMBL; LVJE01000019; OAB27211.1; -; Genomic_DNA.
DR RefSeq; WP_066081560.1; NZ_LVJE01000019.1.
DR AlphaFoldDB; A0A167WBW7; -.
DR STRING; 249352.SAMN05444395_104148; -.
DR OrthoDB; 1521937at2; -.
DR Proteomes; UP000077164; Unassembled WGS sequence.
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 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; 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 51..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 266..294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 733..761
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 806..824
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 836..855
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..75
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 864 AA; 95058 MW; E096F63637E3090A CRC64;
MNWHVLPISK ITQLLNTNPS GITPVVAAER LREQGKNQIE DTKKKSIFKM ILSQFSDFMI
LILVAAAIIS GIIGDVTDTI IILAIVIINA AVGFIQEYRA EKAMEALKNM AANHAHILRE
GKMMSIPATD LVAGDVVLLE AGNIIPADVR FFETHQTKVD ESTLTGESNN LEKNTEELPE
GNYALGDQTN MGFKGTSVTN GRGLAYVVAT GMQTELGRIA KMIQTDETTT PLQKRLAAFG
KRLSVGILLI CTVIFIIGWL RGEAILTMLI TSISLAVAAI PEALPALVTI ALAFGAKKLA
KHKALIRKLP AVETLGSVTY ICSDKTGTLT LNKMTVQEFY ETSTTNYHTV FKDKNRLLQA
IALNNDVSKE ENGKWLGDST EVALVEYAFD KNFNRGDLEK IYPRIAELPF DSKRKCMTTI
HQISTPEDNQ SATMIVLTKG AVDVLFDKLN ADQKSHIPEL ERKVNEMAAK GYRVLGYAMK
TVSSLPQHLD PEEIETELTL IGFVGMIDPP REEARQAVSE CKEAGIIPVM ITGDHKLTAK
AIAAKLGIIS SEEDLALTGS ELAVLNQHEF EEIVAKVRVY ARVNPEQKLR IITALQSKNH
FVAMTGDGVN DAPALKNADI GIAMGINGTE VSKEASHMIL LDDNFATIVI AVKHGRKIFD
NILKFIKYIM TGNSGEIWAI FLAPFFGLPI PLLAIHILWI NLITDGLPGL ALASESAEAN
IMKRPPRNPK ENIFSNGMVV HILWVGFLMG VVTIGMQAYA IHVANSHWQT MAFTVLCFSQ
LGHVMVIRSN NDSIFKIGFF SNKPMIIALA ITVSLQLMII YSPLFNGIFK TQPLTLRELL
VTLAVSSIVF WSVEIEKWLK NRNK
//