ID A0A1I4YAE4_9FLAO Unreviewed; 1075 AA.
AC A0A1I4YAE4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Haloacid dehalogenase-like hydrolase {ECO:0000313|EMBL:SFN35012.1};
GN ORFNames=SAMN05660413_00659 {ECO:0000313|EMBL:SFN35012.1};
OS Salegentibacter flavus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Salegentibacter.
OX NCBI_TaxID=287099 {ECO:0000313|EMBL:SFN35012.1, ECO:0000313|Proteomes:UP000199153};
RN [1] {ECO:0000313|EMBL:SFN35012.1, ECO:0000313|Proteomes:UP000199153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17794 {ECO:0000313|EMBL:SFN35012.1,
RC ECO:0000313|Proteomes:UP000199153};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FOVL01000002; SFN35012.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4YAE4; -.
DR STRING; 287099.SAMN05660413_00659; -.
DR OrthoDB; 1521937at2; -.
DR Proteomes; UP000199153; 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 Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
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; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF29; SECRETORY PATHWAY CALCIUM ATPASE, ISOFORM G; 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 Hydrolase {ECO:0000313|EMBL:SFN35012.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000199153};
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 66..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 254..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 874..898
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 951..973
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1017..1038
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1050..1071
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..86
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 399..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..571
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1075 AA; 119792 MW; 8334449AE265309E CRC64;
MAKEEKSKIV ENAYGKTGEE VIKELSADPD NGLSDKEAKK RKKKYGANVL EEQKERSIWQ
IILAQLNNPI IYLLTAAALL AFLFGDYAEG TAIIIVLIIN TVIGFWMEFK AQKSMEALKN
MDKIEARLLR DGQVKKINAE EIVPGDILLV EAGDLLSADA RILEATELAI DESPLTGESV
PVNKSTEPIE EKTQVADRTN ILYKGTAVTG GTAKAVVYST GMSTELGSIS AMVGEEKKDE
IPLNQKLNKL TRHLIFVTIG LAVAFLIFGY LSGKELYILI QTSIAWTIAA IPEGLPIVAS
IALARGMLRL AEKNVVVKKL EAVETLGETT VIFTDKTGTL TKNQLTVDTF YFPGNVRMSV
DWHSGKQPGM KEKEAPEENP NFKQIFKISV LANDAMLDGE EENQESIEEN SNEEQGKTSK
DAKIEKSAVT AESEDKNTSE EKSNIGKKPK VTSGEDQEKE SSETDHEKKD IDINVDVQKD
GVSVDAKTKN EEDGEKSDMD IDISTSDEGI NIHIRKNTIP KEEKEKPDVS KEENNRKPNK
KDSNDWDDEE IIEEEEEEEE LQEEESENGD DIGENESGKG EGDPLEIALL NYTRKFSKSR
YKKFRNLKRE LHDPFDSESM VMGSVNEDED GEGFYVAGKG AAHAILERSS KVLENGEEKE
LSEKDKEFWN NKNDELSDEG LRVLGFAYRK TNSLPEEEEF LQDLTFAGFI GFLDPPRKEV
AEAINTCREA GIKVIMVTGD HPGTARNVGK QVKLYKNEGD KKSRIINGKE LKEKLENEKD
SGITETSIFS RVDPSQKLSL IKHFQKRGEI VGMTGDGIND APALKRANIG IAMGKRGTQV
AQEVSDMVLK DDTFESIVKA IKQGRIIFGN IRKFIIYQLS YHLSEILIIA SISFGLLALP
LLPLQLLFLN LLSDVFPALA LGVGEGNPGI MKEPPKDPEE PLITKKNWIQ VALYGVILTI
CITGAYLYAH FVWGESEEIT NNVAFFSLAI AQLLHVFNMR EATENIFNNQ VTRNKFIWYA
LAFCAAVLVA AYHIPTISEV LSFHELEMHI WGLILITSIL PLIIIQLIKL IRKDF
//
