ID A0A0P6X4M4_9SPHN Unreviewed; 441 AA.
AC A0A0P6X4M4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=DNA-binding protein {ECO:0000313|EMBL:KPL69011.1};
GN ORFNames=SZ64_13415 {ECO:0000313|EMBL:KPL69011.1};
OS Erythrobacter sp. SG61-1L.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1603897 {ECO:0000313|EMBL:KPL69011.1, ECO:0000313|Proteomes:UP000049978};
RN [1] {ECO:0000313|EMBL:KPL69011.1, ECO:0000313|Proteomes:UP000049978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG61-1L {ECO:0000313|EMBL:KPL69011.1,
RC ECO:0000313|Proteomes:UP000049978};
RA Palumuru S., Dellas N., Pearce S.L., Warden A.C., Oakeshott J.G.,
RA Pandey G.;
RT "Phylogenetic and kinetic characterization of a suite of dehydrogenases
RT from a newly isolated bacterium, strain SG51-1L, that catalyze the turnover
RT of guaiacylglycerol-beta-guaiacyl ether stereoisomers.";
RL Appl. Environ. Microbiol. 0:0-0(2015).
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 -!- SIMILARITY: Belongs to the UPF0053 family. Hemolysin C subfamily.
CC {ECO:0000256|ARBA:ARBA00006446}.
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:KPL69011.1}.
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DR EMBL; JXQC01000003; KPL69011.1; -; Genomic_DNA.
DR RefSeq; WP_054531284.1; NZ_JXQC01000003.1.
DR AlphaFoldDB; A0A0P6X4M4; -.
DR STRING; 1603897.SZ64_13415; -.
DR PATRIC; fig|1603897.4.peg.2629; -.
DR OrthoDB; 9805314at2; -.
DR Proteomes; UP000049978; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR CDD; cd04590; CBS_pair_CorC_HlyC_assoc; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR002550; CNNM.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR044751; Ion_transp-like_CBS.
DR InterPro; IPR005170; Transptr-assoc_dom.
DR PANTHER; PTHR43099:SF5; INTEGRAL MEMBRANE PROTEIN-RELATED; 1.
DR PANTHER; PTHR43099; UPF0053 PROTEIN YRKA; 1.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF01595; CNNM; 1.
DR Pfam; PF03471; CorC_HlyC; 1.
DR SMART; SM01091; CorC_HlyC; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS51846; CNNM; 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW ProRule:PRU00703}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW DNA-binding {ECO:0000313|EMBL:KPL69011.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU01193}; Reference proteome {ECO:0000313|Proteomes:UP000049978};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU01193};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|PROSITE-
KW ProRule:PRU01193}.
FT TRANSMEM 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 67..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..202
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000259|PROSITE:PS51846"
FT DOMAIN 221..282
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 285..345
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 441 AA; 47329 MW; EFC0CDC3F4B52059 CRC64;
MTPFPWIDVL IIAGLILLNG LFAMSELAIV SARPARLQVA AEKGSKAAKA AIDLEADPGK
FLSTVQIGIT LVGIIAGAYS GASLGGPVGE RLGLLGVPDR MADEVGFALV IVLTTYFSLV
VGELVPKQFA LRAAEPIALL MARPMMLLSK VAAPFVWLLD KSSATLMRLL RISHRGEHGL
TAEELQIIFA EATRSGAIEE DERAIMAGIM KLANRPVREL MTPRTELDWI DCSASEAEIR
ATIAASPHSL LPVADGSTDK VVGVVKVREV LALLLEKKTI DLDSVLRKPE VIPDQLDAMD
ALRMLQQSGT GMAMVHDEYG HLEGVVTPAD LLMALVGTFV SHQDEGDAPQ LVERADGSLL
VAGYMPADLM ADRLGIELPE DREFATAAGF VLAVLKKLPT VGEVFETQGW RFEVVDMDGL
RIDQLLVSQL NDEAPEPDTG D
//
