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Database: UniProt
Entry: Q1YL12_AURMS
LinkDB: Q1YL12_AURMS
Original site: Q1YL12_AURMS 
ID   Q1YL12_AURMS            Unreviewed;       668 AA.
AC   Q1YL12;
DT   02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   02-MAY-2006, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   SubName: Full=Conserved hypothetical membrane protein {ECO:0000313|EMBL:EAS50959.1};
GN   ORFNames=SI859A1_01764 {ECO:0000313|EMBL:EAS50959.1};
OS   Aurantimonas manganoxydans (strain ATCC BAA-1229 / DSM 21871 / SI85-9A1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Aurantimonadaceae; Aurantimonas.
OX   NCBI_TaxID=287752 {ECO:0000313|EMBL:EAS50959.1, ECO:0000313|Proteomes:UP000000321};
RN   [1] {ECO:0000313|EMBL:EAS50959.1, ECO:0000313|Proteomes:UP000000321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SI85-9A1 {ECO:0000313|EMBL:EAS50959.1,
RC   ECO:0000313|Proteomes:UP000000321};
RX   PubMed=18344346; DOI=10.1128/AEM.01656-07;
RA   Dick G.J., Podell S., Johnson H.A., Rivera-Espinoza Y., Bernier-Latmani R.,
RA   McCarthy J.K., Torpey J.W., Clement B.G., Gaasterland T., Tebo B.M.;
RT   "Genomic insights into Mn(II) oxidation by the marine alphaproteobacterium
RT   Aurantimonas sp. strain SI85-9A1.";
RL   Appl. Environ. Microbiol. 74:2646-2658(2008).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the DedA family.
CC       {ECO:0000256|ARBA:ARBA00010792}.
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:EAS50959.1}.
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DR   EMBL; AAPJ01000001; EAS50959.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1YL12; -.
DR   HOGENOM; CLU_025730_2_0_5; -.
DR   BioCyc; AURANTIMONAS:SI859A1_01764-MONOMER; -.
DR   Proteomes; UP000000321; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   CDD; cd03392; PAP2_like_2; 1.
DR   Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR   InterPro; IPR032818; DedA.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   InterPro; IPR032816; VTT_dom.
DR   PANTHER; PTHR30353; INNER MEMBRANE PROTEIN DEDA-RELATED; 1.
DR   PANTHER; PTHR30353:SF15; INNER MEMBRANE PROTEIN YABI; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   Pfam; PF09335; SNARE_assoc; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000321};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        157..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        190..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        254..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        301..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        333..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        363..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        402..423
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        429..449
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        456..476
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          333..444
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
SQ   SEQUENCE   668 AA;  71594 MW;  A96FBC83636F1A27 CRC64;
     MLACPQHAPK KLMTQTLLSL VDQHLLLAYT FLFAVCLGEA LFIIGLFVPS TVVLIAVGAM
     IGGGKLPFMP VLVVAAAGAT AGDALSYAIG HHYRDRLRTV WPFRRYGTLI ERGEAFFHRH
     GGKSVFLGRF VPGVKAIVPG IAGMVGMGVV RFTSVNVASA FVWATAHLIP AAGIGIGLSR
     VHSLDPRLAI LLVGAIAVLL LAWYVGKIAI AFVWPVAADW RRVRIERRAN STSRLARLEL
     RYLSNDDNIV GRTAIMVVAA LAAAGFLLLL GNLLFDPELK LADKAVYNFL QSYRSDAGTK
     IVTAITMAAD GFVLTSLTVA IVLWLAIRRH IRVAIAAALA MAGSELFVHL VKGTIERPRP
     TDLYAGVSSF SFPSGHATLS MTFFGILAVI VASHMKPGSR PIVLGIAALA ALTVAFSRLY
     LGAHWLTDVS AGMSFGILMA AVFALTTHLR DRTIRLVPLV VVLLAVFAGS YGSHLWRDYG
     IWIRNYAPMR LTTDMSKDEW LKDGWKSLAS HRLTMGGDAA GPILFQTDLD VAELAPLLAS
     AGWSPMTTGG LAQALLPSAG PLPERAALPL LHEGRMPVAT FTHPSQDGRD VLTLWPSAYR
     LGPDGSERPI LLAGYSKEVV DPFVLGLAFV AVKPEAVPPD TATRPLAALV RAHPTDLVPL
     PSGPAQRR
//
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