ID A0A160F4E5_9BACI Unreviewed; 420 AA.
AC A0A160F4E5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=CBS domain protein {ECO:0000313|EMBL:ANB60891.1};
GN ORFNames=GFC30_1004 {ECO:0000313|EMBL:ANB60891.1};
OS Anoxybacillus amylolyticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=294699 {ECO:0000313|EMBL:ANB60891.1, ECO:0000313|Proteomes:UP000076865};
RN [1] {ECO:0000313|EMBL:ANB60891.1, ECO:0000313|Proteomes:UP000076865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15939 {ECO:0000313|EMBL:ANB60891.1,
RC ECO:0000313|Proteomes:UP000076865};
RX PubMed=16682297; DOI=10.1016/j.syapm.2005.10.003;
RA Poli A., Esposito E., Lama L., Orlando P., Nicolaus G., de Appolonia F.,
RA Gambacorta A., Nicolaus B.;
RT "Anoxybacillus amylolyticus sp. nov., a thermophilic amylase producing
RT bacterium isolated from Mount Rittmann (Antarctica).";
RL Syst. Appl. Microbiol. 29:300-307(2006).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the UPF0053 family.
CC {ECO:0000256|ARBA:ARBA00006337}.
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DR EMBL; CP015438; ANB60891.1; -; Genomic_DNA.
DR RefSeq; WP_066323153.1; NZ_CP015438.1.
DR AlphaFoldDB; A0A160F4E5; -.
DR KEGG; aamy:GFC30_1004; -.
DR PATRIC; fig|294699.3.peg.995; -.
DR OrthoDB; 9798188at2; -.
DR Proteomes; UP000076865; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; PTHR22777; HEMOLYSIN-RELATED; 1.
DR PANTHER; PTHR22777:SF17; UPF0053 INNER MEMBRANE PROTEIN YFJD; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01595; CNNM; 1.
DR Pfam; PF03471; CorC_HlyC; 1.
DR SMART; SM00116; CBS; 2.
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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU01193}; Reference proteome {ECO:0000313|Proteomes:UP000076865};
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 92..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..187
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000259|PROSITE:PS51846"
FT DOMAIN 206..265
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 270..327
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 420 AA; 47284 MW; B8C6FDB9460C670F CRC64;
MGELPLIFSL LLFFIALSAF FSSAEAAFSA VSKMRLKHDA GEQIDDNRRT VYIAEHLEEV
LLTAVVANHF VKAVAIVFSV KIASTLFGET TGLWIGALVI IVLLLMFSEI IPKTIAEEHA
ESVALKYAGI MYALMKAMFP LTWLFVGLKG KLVRRLTDGM ISPSMTEEEI KEMIDLSEEE
GVIDNKEKEL VHRSLDFDDI LVGEIFTPRI DMVAVEVNDS VEKIRDVFLQ ERYSRVPVYE
DDIDHVIGIL SESDFLSQLV QQKEVNIRAL LRKPLFVVES MKIADLLPAL QKSKVHMAIV
VDEFGGTAGL ITLEDIIEQI VGEIWDEHDD AIKVIQQIDD YSYEMNAELP LDEFCEFMKM
DEPESSSHTL GGWVFELLGR IPTGGETVQY GSLTLTVRQV ENRRIRKVLV SLNEPIAEEV
//
