ID A0A0A7FZN5_9CLOT Unreviewed; 840 AA.
AC A0A0A7FZN5;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=HAD ATPase, P-type, IC family protein {ECO:0000313|EMBL:AIY85057.1};
GN ORFNames=U729_1929 {ECO:0000313|EMBL:AIY85057.1};
OS Clostridium baratii str. Sullivan.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1415775 {ECO:0000313|EMBL:AIY85057.1, ECO:0000313|Proteomes:UP000030635};
RN [1] {ECO:0000313|EMBL:AIY85057.1, ECO:0000313|Proteomes:UP000030635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sullivan {ECO:0000313|EMBL:AIY85057.1};
RX PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA Karavis M.A., Smith L.A.;
RT "Genomic sequences of six botulinum neurotoxin-producing strains
RT representing three clostridial species illustrate the mobility and
RT diversity of botulinum neurotoxin genes.";
RL Infect. Genet. Evol. 30:102-113(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP006905; AIY85057.1; -; Genomic_DNA.
DR RefSeq; WP_039314180.1; NZ_CP006905.1.
DR AlphaFoldDB; A0A0A7FZN5; -.
DR STRING; 1561.NPD11_1085; -.
DR KEGG; cbv:U729_1929; -.
DR eggNOG; COG0474; Bacteria.
DR HOGENOM; CLU_002360_2_1_9; -.
DR OrthoDB; 9760364at2; -.
DR Proteomes; UP000030635; 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 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:SF156; CALCIUM-TRANSPORTING 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 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:UP000030635};
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 44..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 69..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 633..654
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 660..683
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 704..729
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 741..760
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 780..802
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 814..831
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 3..65
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 840 AA; 93521 MW; 679F747243A32C3C CRC64;
MAQEKNYNMK GLTNEEVKLA REKFGKNVLI EEKKENFLMK VVEVIKEPMF LLLMVAAIIY
FILGEPKDGS IMLIFVVGVI SIEVIQEWKT DKTLKALKNL SAQHIEVIRE FKRITINSEE
LVPGDLMIIT EGIKIPADGK VVYSNDLCVN ESSLTGEALG VWKCSECTDE NKQYFRKDYC
YAGTLVIQGS GVILVKKIGA NTEYGKIGKN VSENIEEDTL LQKQTGKLVK VCAGIAGILF
ALVSGITYLN LQDVVFEDRI IQSILSGVTL AMAMIPEEFP VVLTVFLSMG AWRLAKKNSL
VRKLPSVETL GAISVLCVDK TGTITMNEMT IDEAWSIDEN VKHLLEVMGM ACETEAYDPM
EKAMIKYCEK NNILKEFLFN GELVTEYSFT HENKMMGHVW KREEGIIVAA KGSPEKILNI
CDLNNEDHKK IEDKIYNMSS KGLRVIAVGK MDIDDESDIK NTLEECTLKF LGLVGLLDPP
REGIKDDIET CNRAGIRVVM ITGDNGITAS SIARKVGISH SGEIITGDEL DKMSDDELRE
KVKHTNIFSR VIPEHKMRIV KAFKENGEVV GMTGDGVNDA PALKYADIGI AMGKRGSEVS
REAADLILLD DNFSTIVDTV KDGRRIYDNI RRAIGYIFTI HIPIAFSAII APILGIGSSM
LLLLPVHVVL LELIIDPTCS IVLEREPAES DIMRRKPRNP NEGILTKDVL IKSIIQGVVM
FLASFGTYYI YYKCNSGDIN IARTMGLSII IISNILLVYV NSSSNELVYK SFNNLIKDKV
MWGVNGGTII GLLVIMYTPI SGFLKLAPLG IKDFLIVIAV SIIAVMWYEI VKIFKKKKQR
//
