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Database: UniProt
Entry: Q92DI1_LISIN
LinkDB: Q92DI1_LISIN
Original site: Q92DI1_LISIN 
ID   Q92DI1_LISIN            Unreviewed;       882 AA.
AC   Q92DI1;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 137.
DE   SubName: Full=Lin0832 protein {ECO:0000313|EMBL:CAC96064.1};
GN   OrderedLocusNames=lin0832 {ECO:0000313|EMBL:CAC96064.1};
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626 {ECO:0000313|EMBL:CAC96064.1, ECO:0000313|Proteomes:UP000002513};
RN   [1] {ECO:0000313|EMBL:CAC96064.1, ECO:0000313|Proteomes:UP000002513}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262 {ECO:0000313|Proteomes:UP000002513};
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.D.,
RA   Fsihi H., Portillo F.G., Garrido P., Gautier L., Goebel W., Gomez-Lopez N.,
RA   Hain T., Hauf J., Jackson D., Jones L.M., Kaerst U., Kreft J., Kuhn M.,
RA   Kunst F., Kurapkat G., Madueno E., Maitournam A., Vicente J.M., Ng E.,
RA   Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.C.,
RA   Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
RA   Vazquez-Boland J.A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; AL596166; CAC96064.1; -; Genomic_DNA.
DR   PIR; AH1536; AH1536.
DR   RefSeq; WP_010990634.1; NC_003212.1.
DR   AlphaFoldDB; Q92DI1; -.
DR   STRING; 272626.gene:17565159; -.
DR   KEGG; lin:lin0832; -.
DR   eggNOG; COG0474; Bacteria.
DR   HOGENOM; CLU_002360_3_3_9; -.
DR   OrthoDB; 9813266at2; -.
DR   Proteomes; UP000002513; 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:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR   CDD; cd02089; P-type_ATPase_Ca_prok; 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; 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; PF08282; Hydrolase_3; 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   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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:ARBA00022448}.
FT   TRANSMEM        50..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        79..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        243..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        276..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        681..701
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        707..727
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        748..770
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        814..834
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        854..874
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   882 AA;  95875 MW;  232FA2C85F89AB13 CRC64;
     MEIYRKSAAD TFKQLEATEQ GLTTSEVTKR QEKYGFNELK NKKKDPLWKL FLETFKDPMV
     IVLVIAALVQ LVLGEVVESL IIFLVLIVNS IISVVQTRKA ESSLDALREM SAPVAKVIRD
     GSKQSIHARE LVPGDVVILD AGDFVPADGR LFESGSLKID EGMLTGESEA VEKYIDTISD
     EVGLGDRVNM VFSGSLVVYG RGMFVVTGTA SETEIGKIAG LLETAEAKQT PLQRKLESFS
     KKLGIGILAL CVLIFAVEAG RVLLGDNSAD MATAILNAFM FAVAVAVAAI PEALSSIVTI
     VLAVGTNKMA KQHAIIRKLP AVETLGSTSV ICTDKTGTLT QNKMTVVDYF LPDGTKENFP
     DSPENWSEGE RRLIHIAVLC NDSNINSEGK ELGDPTEVAL IAFSNKNNQD YNEIREKFIR
     EGEIPFDSDR KLMSTLHTFN ENKAMLTKGG PDVMFARCSY VFLDGEEKPM TEEILTKLKE
     TNEEFSNQAL RVLAYGYKRM PADTTELKLE DEQDIVLVGL TAMIDPPREA VYASIEESKK
     AGIRTVMITG DHKTTAQAIG RDIGLMDADD IALTGQELDA MPEEELDKKL EHIAVYARVS
     PENKIRIVKA WQKKGKITAM TGDGVNDAPA LKQADIGVAM GSGTDVAKDS AAMILTDDNF
     VSIVDAVGVG RTVFDNIKKS IAYLFAGNLG AIIAILFALV LDWINPFTAL QLLFINLVND
     SLPAIALGME KAEPDVMKRK PRDINEGIFA GGTMRAVISR GVLIGIAVII SQYIGMQISP
     EMSVAMAFTT LILARTLQTF AARSNVQTAF GAGFFSNKYV IGAVLLCFVL YGITVLPGAR
     EIFSIPATFG LHEWSIAAGL ALAAVVMMEI IKVVQNKFFK EA
//
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