ID A9LZF1_NEIM0 Unreviewed; 842 AA.
AC A9LZF1;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=P-type cation-transporting ATPase {ECO:0000313|EMBL:ABX73327.1};
GN OrderedLocusNames=NMCC_1153 {ECO:0000313|EMBL:ABX73327.1};
OS Neisseria meningitidis serogroup C (strain 053442).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=374833 {ECO:0000313|EMBL:ABX73327.1, ECO:0000313|Proteomes:UP000001177};
RN [1] {ECO:0000313|EMBL:ABX73327.1, ECO:0000313|Proteomes:UP000001177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=053442 {ECO:0000313|EMBL:ABX73327.1,
RC ECO:0000313|Proteomes:UP000001177};
RX PubMed=18031983; DOI=10.1016/j.ygeno.2007.10.004;
RA Peng J., Yang L., Yang F., Yang J., Yan Y., Nie H., Zhang X., Xiong Z.,
RA Jiang Y., Cheng F., Xu X., Chen S., Sun L., Li W., Shen Y., Shao Z.,
RA Liang X., Xu J., Jin Q.;
RT "Characterization of ST-4821 complex, a unique Neisseria meningitidis
RT clone.";
RL Genomics 91:78-87(2008).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362081}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000256|ARBA:ARBA00006024,
CC ECO:0000256|RuleBase:RU362081}.
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DR EMBL; CP000381; ABX73327.1; -; Genomic_DNA.
DR AlphaFoldDB; A9LZF1; -.
DR KEGG; nmn:NMCC_1153; -.
DR HOGENOM; CLU_001771_0_3_4; -.
DR Proteomes; UP000001177; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR CDD; cd00371; HMA; 1.
DR CDD; cd02079; P-type_ATPase_HM; 1.
DR Gene3D; 3.30.70.100; -; 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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR021993; ATPase-cat-bd.
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; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF5; CATION-TRANSPORTING P-TYPE ATPASE-RELATED; 1.
DR Pfam; PF12156; ATPase-cat_bd; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00943; CUATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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; SSF55008; HMA, heavy metal-associated domain; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}.
FT TRANSMEM 188..211
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 223..244
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 256..278
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 284..303
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 441..463
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 469..488
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 779..798
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 804..822
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 104..170
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 842 AA; 91595 MW; 2E9051FE55B3F071 CRC64;
MCHRTKHRRN RNAMKKTCFH CGLDVPENLH LTVRYENEDR ETCCAGCQAV AQSIIDAGLG
SYYKQRTADA QKTELPPQEI LDQIRLYDLP EVQSDFVETH GGTREAVLML GGITCAACVW
LIEQQLLRTD GIVRIDLNYS THRCRVVWDD GKIRLSDILL KIRQIGYTAA PYDAQKIEAA
NQKERKQYIV RLAVAGLGMM QTMMFALPTY LYGGDIEPDF LQILHWGGFL MVLPVVFYCA
VPFYQGALRD LKNRRAGMDT PIAVAIIMTF IAGVYSLATN AGQGMYFESI AMLLFFLLGG
RFMEHIARRK AGDAAERLVK LIPAFCHHMP DYPDTQETCE AAVVKLKAGD IVLVKPGETI
PIDGTVLEGA STVDESMLTG ESLPVAKMPS EKVTAGTLNT QNPLIIRTDR TGGGTRLSHI
VRLLDRALAQ KPRTAELAEQ YASSFIFGEL LLAVPVFIGW TLYADAHTAL WITVALLVIT
CPCALSLATP TALAASTGTL AREGILIGGK QAIETLAQTT DIIFDKTGTL TQGKPAVRRI
SLLRGTDEAF VLAVAQALEQ QSEHPLARAI LNCRISDGSV PDIAIKQRLN RIGEGVGAQL
TVNGETQVWA LGRASYVAEI SGKEPQTEGG GSAVYLGSQS GFQAVFYLTD PLKDSAAEAV
RQLAGKNLTL HILSGDRETA VAETARALGV AHYRAQAMPE DKLEYVKALQ KEGKKVLMIG
DGINDAPVLA QADVSAAAAG GTDIARDGAD IVLLNEDLNI VPHMFAQARR TQQIIRQNLI
WAGAYNIIAV PLAVLGYVQP WIAALGMSFS SLAVLGNALR LHKRGKMPSE KMPSEQCRTA
LL
//
