ID A0A0W0VN57_9GAMM Unreviewed; 899 AA.
AC A0A0W0VN57;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Cation efflux transporter {ECO:0000313|EMBL:KTD21177.1};
GN Name=pacL {ECO:0000313|EMBL:KTD21177.1};
GN ORFNames=Llon_1275 {ECO:0000313|EMBL:KTD21177.1};
OS Legionella londiniensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45068 {ECO:0000313|EMBL:KTD21177.1, ECO:0000313|Proteomes:UP000054997};
RN [1] {ECO:0000313|EMBL:KTD21177.1, ECO:0000313|Proteomes:UP000054997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49505 {ECO:0000313|EMBL:KTD21177.1,
RC ECO:0000313|Proteomes:UP000054997};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KTD21177.1}.
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DR EMBL; LNYK01000016; KTD21177.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0VN57; -.
DR STRING; 45068.Llon_1275; -.
DR PATRIC; fig|45068.5.peg.1380; -.
DR Proteomes; UP000054997; 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 GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
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; 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; 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:UP000054997};
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 57..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 690..715
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 721..739
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 759..786
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 798..818
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 830..850
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 862..881
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..77
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 899 AA; 98548 MW; 04A1539EF89AF79A CRC64;
MSKNWHAEPA EKALITLGTG AKGLNANEVR DRQAIFGFNQ IPAAAKETIL VRFLRHFNHL
LIYVLLIAAV TTALLRHWVD TVVILLVVIV NAFIGFIQEG KAEKALDAIR HMLSPMADVL
RGGERQRIPA KELVPGDIVL LEAGDKVPAD IRLIKAHGLN IDESVITGES VSVEKDTKPV
AQDAVLGERS SMAYSGTLVT RGTGAGVVVA TGLYSEIGKI SGLLAKVELL KTPLVRQMDI
FAKWLTILIL MVAALLLIFG YFVQHYNFSE LFMIVVGLSV AAIPEGLPAV LSITLAVGVQ
AMARRHAIIR RLPAIETIGS VSVICTDKTG TLTRNEMTVV SALTANHFYE VEGSGYLPVG
SIKLHGEIIN PNKHPSLLRL IQCSVLCNAA TLYHRQGSWQ IEGDPMEASL LVLAEKAGIP
INEIRQTWAS TDIIPFDARH RFMATLHHNH QGHAYIFVKG APEQLLTLCQ NQQSDRGDQE
AVNQAYWLQK VEETAKKGQR VLAFAMKSIP ADKTVLQMQD VQEGLVLLGM TGMIDPPREE
AIIAVGQCID AGIHVKMITG DHAVTAEAIG RQIGLEHPDK ILKGFEIDAM NDMELANAVL
ENDIFARTSP EHKLRLVMAL QSHGMVVAMT GDGVNDALAL KRADVGIAMG QKGNEVSKEA
AELILTDDNF ASIAAAVQEG RTVYDNLKKV ISWTLPTNAG EAMTIILALL LGLSLPVTPI
QILWINLITT VTLGLSLAFE PTEDNTMHRP PRPRNEPILT GALAWHIVLV SFLFVCGVFG
IYYYVLDKGY SLELSRTIAL NTLVVLEIFH LFYIRNIYGT SLTWHAVKGT RVVWISIIVI
TIAQFSITYL PFMQHIFSTE AIPFFDGALV IAIGVVFFAL IETEKQLRLR IISLRHPNI
//
