ID D5BMW1_PUNMI Unreviewed; 421 AA.
AC D5BMW1;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=CBS domain protein {ECO:0000313|EMBL:ADE40154.1};
DE EC=2.3.1.28 {ECO:0000313|EMBL:ADE40154.1};
GN OrderedLocusNames=SAR116_1911 {ECO:0000313|EMBL:ADE40154.1};
OS Puniceispirillum marinum (strain IMCC1322).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; SAR116 cluster;
OC Puniceispirillum.
OX NCBI_TaxID=488538 {ECO:0000313|EMBL:ADE40154.1, ECO:0000313|Proteomes:UP000007460};
RN [1] {ECO:0000313|EMBL:ADE40154.1, ECO:0000313|Proteomes:UP000007460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC1322 {ECO:0000313|EMBL:ADE40154.1,
RC ECO:0000313|Proteomes:UP000007460};
RX PubMed=20382761; DOI=10.1128/JB.00347-10;
RA Oh H.M., Kwon K.K., Kang I., Kang S.G., Lee J.H., Kim S.J., Cho J.C.;
RT "Complete genome sequence of "Candidatus Puniceispirillum marinum"
RT IMCC1322, a representative of the SAR116 clade in the
RT Alphaproteobacteria.";
RL J. Bacteriol. 192:3240-3241(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the UPF0053 family. Hemolysin C subfamily.
CC {ECO:0000256|ARBA:ARBA00006446}.
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DR EMBL; CP001751; ADE40154.1; -; Genomic_DNA.
DR AlphaFoldDB; D5BMW1; -.
DR STRING; 488538.SAR116_1911; -.
DR KEGG; apb:SAR116_1911; -.
DR eggNOG; COG4536; Bacteria.
DR HOGENOM; CLU_015237_4_1_5; -.
DR Proteomes; UP000007460; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008811; F:chloramphenicol O-acetyltransferase activity; IEA:UniProtKB-EC.
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; 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 Acyltransferase {ECO:0000313|EMBL:ADE40154.1};
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:UP000007460};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:ADE40154.1};
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..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 62..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 94..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..189
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000259|PROSITE:PS51846"
FT DOMAIN 205..267
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 278..338
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 421 AA; 46572 MW; 82895AE168E956E4 CRC64;
MMSDSLWTIS ALIVILILAS AFFSSAETAL TAASDARMRQ LATKGNKNAK IVESLRADRE
GLIGAILIGN NAVNVLASAI ATSLFITLYG EAGLLWATIT MTVLLVVFAE VMPKTYALTY
ADRYALTIAP VIRIVVLALS PLALAIRWLA SITIRARSDE DTDREEELRG LIELHGADGD
DDDRETQAML SSILDLNELT VEQIMTHRGS VNMINAEDDL DDILRRVLES PHTRHPVFAG
TSDNIIGVLH VKDLLRSIGH LGENVSENGN GNKFVQDIAS PAYFIPETTL LFDQLQSFRS
RREHFAVVVD EYGDFRGIVT LEDILEEIVG DIDDEHDIDL PGLTPQADGS WLVDGSVTIR
DLNRALGWQL PDEDASTLAG LVLFESRTIP MPGQEFRFHN IRFRVVKRDG NRITSLRLWS
H
//
