ID A0A022L1D9_9MICO Unreviewed; 911 AA.
AC A0A022L1D9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Carbonate dehydratase {ECO:0000313|EMBL:EYT49596.1};
GN ORFNames=D641_0107080 {ECO:0000313|EMBL:EYT49596.1};
OS Brachybacterium muris UCD-AY4.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=1249481 {ECO:0000313|EMBL:EYT49596.1, ECO:0000313|Proteomes:UP000019754};
RN [1] {ECO:0000313|EMBL:EYT49596.1, ECO:0000313|Proteomes:UP000019754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-AY4 {ECO:0000313|EMBL:EYT49596.1,
RC ECO:0000313|Proteomes:UP000019754};
RX PubMed=23516213;
RA Lo J.R., Lang J.M., Darling A.E., Eisen J.A., Coil D.A.;
RT "Draft genome sequence of an Actinobacterium, Brachybacterium muris strain
RT UCD-AY4.";
RL Genome Announc. 1:E0008613-E0008613(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00001836};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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:EYT49596.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AORC01000008; EYT49596.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A022L1D9; -.
DR STRING; 1249481.D641_0107080; -.
DR HOGENOM; CLU_002360_3_2_11; -.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000019754; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; 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; 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 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:UP000019754};
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 83..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 711..732
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 744..763
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 784..809
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 815..833
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 853..873
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 885..902
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..99
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 911 AA; 97067 MW; 415B4CDB616BE300 CRC64;
MTTATASPEQ PPTHDQQRDE QSVVPDPHAV GTEQAMEVLE VSGDGLTADA AAARLERYGP
NALPSGEQES ALTRLLRQFR DPMIYVLIGA AVLTTVMGHY VDTIVIAAVV IINAVIGYLQ
EGKAADALDG IRTMLSLEAQ ARRDGTWVTV PADELVPGDV VRLAAGDKVP ADLRILEATN
LTCEESALTG ESVPVEKGTD PVEADAGLGD RTSMAFSGTT VASGSGRGLV VGTGRRTEIG
HITTMLDEVE SMETPLTRQM ASFSTKLSLL VVIAAVLMFG IGWVLYDYSL ADLTLSAIGF
AVAAIPEGLP AVLTITLALG VQKMAGRNSI TRRMNSVETL GSVTVICSDK TGTLTRNEMT
VRTVVTPEGT YEVSGTGYAP EGDIEQDGAA VGPEERNDLR MLAEVAARTN DSTVSRKDDR
WVLSGEPTDG GLRTFAMKAG IEGHDENRID AVPFDSAYKY MATLDRIDGI GDVVNLKGAP
DRLLDRCDRQ GVDLDENEPL DREHWERAID ELSGQGLRVL AAAVRRADDR GSATSLTTDD
IDGGGFVFLG LYGIIDPPRE EAMDAIRACH DAGIRVVMIT GDHAGTASAI GREMGIEDEQ
GAVTGNQLEE ASDEELAQLA RTHSVFARTS PEHKLRLVQA LQDDGEVVSM TGDGVNDAPS
LKRADVGVAM GIKGTEATKD AADVVLADDN FATIADAVQM GRTIYDNLRK AIVFILPTNG
AQGLVVLVSV LLGMTLPLTP VQVLWVNTIT AVTLALALAF EPGEPDIMRR PPRDPKESIL
PRAGVVRIVY VSLLLGAVTI GVFLLGQAAG VSLEISRTTA VNTLVVGQIF YLLASRFTRT
TSLRKELLTT NPISWLCIAV MLLLQLAFVY VPFMQTTFAS GPVGWMGWLV PLGAGVLVFA
VVEADKALRR R
//
