ID D3HN87_LEGLN Unreviewed; 899 AA.
AC D3HN87;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=P-type Ca(2+) transporter {ECO:0000256|ARBA:ARBA00012790};
DE EC=7.2.2.10 {ECO:0000256|ARBA:ARBA00012790};
GN OrderedLocusNames=LLO_0022 {ECO:0000313|EMBL:CBJ10343.1};
OS Legionella longbeachae serogroup 1 (strain NSW150).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=661367 {ECO:0000313|EMBL:CBJ10343.1, ECO:0000313|Proteomes:UP000001060};
RN [1] {ECO:0000313|EMBL:CBJ10343.1, ECO:0000313|Proteomes:UP000001060}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSW150 {ECO:0000313|EMBL:CBJ10343.1,
RC ECO:0000313|Proteomes:UP000001060};
RX PubMed=20174605; DOI=10.1371/journal.pgen.1000851;
RA Cazalet C., Gomez-Valero L., Rusniok C., Lomma M., Dervins-Ravault D.,
RA Newton H., Sansom F., Jarraud S., Zidane N., Ma L., Bouchier C.,
RA Etienne J., Hartland E., Buchrieser C.;
RT "Analysis of the Legionella longbeachae genome and transcriptome uncovers
RT unique strategies to cause Legionnaires' disease.";
RL PLoS Genet. 6:E1000851-E1000851(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FN650140; CBJ10343.1; -; Genomic_DNA.
DR AlphaFoldDB; D3HN87; -.
DR KEGG; llo:LLO_0022; -.
DR eggNOG; COG0474; Bacteria.
DR HOGENOM; CLU_002360_3_3_6; -.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000001060; 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 GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
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; IPR006408; P-type_ATPase_IIB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
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; 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; SFLDG00002; C1.7:_P-type_atpase_like; 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 Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568};
KW Ion transport {ECO:0000256|ARBA:ARBA00022568};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001060};
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}; Transport {ECO:0000256|ARBA:ARBA00022568}.
FT TRANSMEM 65..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 96..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 290..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 699..719
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..820
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 840..859
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 865..887
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 18..92
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 899 AA; 98447 MW; 258755BAF90A217D CRC64;
MQLNVKSEKD PDMTQTESWH TFEISEVALH LNVDLSKGLS DQEAATRLAS VGINQIQNQS
SRSPLLVFLA QFKSALILIL IGASVLATLI GNFKDASVIL AIVVINAFVS FYQEYRAEQS
LAALRKMLPV QAHVRRSGKK YTINAASLVP GDIVLVEAGD RLPADGRLVV VANFDVDEST
LTGESQPVRK YVDAMFERDA PIADRLNMAY MNTMVTRGRA ELLVTATGMH TEMGKLSQQL
ALTPEILSPL QVQLDQLGKR LGAIALLLIS LLFVFQLFRG ENVTHAIIDA IVLAVAAMPE
GLPVVVTVTL ALGMHQMARH RAIVKRLASV EILGCTTVIC SDKTGTLTLN QMTVRELFYL
GQRFKVTGEG YSTSGAVLHE TRNSVLPDMQ PLLVPLVACN DSHIEDERVI GDPTEAALLV
LTVKAGLHHE QVLTEYPRIA EIPFDSTYKF MATFHRVGRG GQIFVKGAPD VLLARCSHFF
SDDHNVLLDS KHKEEIEEQY CTMASRGLRC LLIASRTLDA DEFVLSDNLF VWIGDLTFIG
LIGLQDPPRT EAKQAIAQCK QAGIAVKMIT GDHTDTGVAI AHELGLQGEA ISGKELDRLD
DLQLAEVINN ITVFARVSPA HKVKIVQVLQ SKGHVVAMTG DGLNDAPALK NADIGVAMGV
VGTEVAKEAA TMVLMDDNFS TIVSAVEQGR VLYDNILKFI RFQLSTTVGA ILTVFFAPIL
GLPEPFNPIQ ILWVALIMDG PPAVSLALDA GRPGIMNDSP RNRLEPVLPW MRLARIFVFG
ITMMVGTLGV LYYAVNNYNE QTALTLAFTT FVLFQFFNVF NARVEKGSAF GKGFFQNRML
WLSLTAVVIL QVLAVHWIPA QSIFGTSYLT LAQWLMAIGI ASSILIFEEG RKAAIRWFL
//
