ID C3SCW0_ECOLX Unreviewed; 549 AA.
AC C3SCW0;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Putative transport protein {ECO:0000313|EMBL:ACI72317.1};
GN ORFNames=ECs2868 {ECO:0000313|EMBL:ACI72317.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:ACI72317.1};
RN [1] {ECO:0000313|EMBL:ACI72317.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=86-24 {ECO:0000313|EMBL:ACI72317.1}, 87-14
RC {ECO:0000313|EMBL:ACI72318.1}, and TW14359
RC {ECO:0000313|EMBL:ACI72319.1};
RX PubMed=19439656; DOI=10.1073/pnas.0812949106;
RA Leopold S.R., Magrini V., Holt N.J., Shaikh N., Mardis E.R., Cagno J.,
RA Ogura Y., Iguchi A., Hayashi T., Mellmann A., Karch H., Besser T.E.,
RA Sawyer S.A., Whittam T.S., Tarr P.I.;
RT "A precise reconstruction of the emergence and constrained radiations of
RT Escherichia coli O157 portrayed by backbone concatenomic analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8713-8718(2009).
CC -!- SIMILARITY: Belongs to the UPF0053 family.
CC {ECO:0000256|ARBA:ARBA00006337}.
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DR EMBL; EU889725; ACI72317.1; -; Genomic_DNA.
DR EMBL; EU889726; ACI72318.1; -; Genomic_DNA.
DR EMBL; EU889727; ACI72319.1; -; Genomic_DNA.
DR AlphaFoldDB; C3SCW0; -.
DR GO; GO:0016020; C:membrane; 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; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR005496; Integral_membrane_TerC.
DR InterPro; IPR044751; Ion_transp-like_CBS.
DR InterPro; IPR005170; Transptr-assoc_dom.
DR PANTHER; PTHR22777; HEMOLYSIN-RELATED; 1.
DR PANTHER; PTHR22777:SF33; UPF0053 PROTEIN YEGH; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF03471; CorC_HlyC; 1.
DR Pfam; PF03741; TerC; 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.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW ProRule:PRU00703}; Membrane {ECO:0000256|SAM:Phobius};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 206..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 328..388
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 393..451
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 549 AA; 62077 MW; 2A300AFCA60FD6BF CRC64;
MPRFIHDRIV TFVIQRIGFV LTMEWIADPS IWAGLITLIV IELVLGIDNL VFIAILAEKL
PPKQRDRARV TGLLLAMLMR LLLLASISWL VTLTQPLFSF RSFTFSARDL IMLFGGFFLL
FKATMELNER LEGKDSNNPT QRKGAKFWGV VTQIVVLDAI FSLDSVITAV GMVDHLLVMM
AAVVIAISLM LMASKPLTQF VNSHPTIVIL CLSFLLMIGF SLVAEGFGFV IPKGYLYAAI
GFSVMIEALN QLAIFNRRRF LSANQTLRQR TTEAVMRLLS GQKEDAELDA ETASMLVDHG
NQQIFNPQER RMIERVLNLN QRTVSSIMTS RHDIEHIDLN APEDEIRQLL ERNQHTRLVV
TDGDDAEDLL GVVHVIDLLQ QSLRGEPLNL RVLIRQPLVF PETLPLLPAL EQFRNARTHF
AFVVDEFGSV EGIVTLSDVT ETIAGNLPNE VEEIDARHDI QKNADGSWTA NGHMPLEDLV
QYVPLPLDEK REYHTIAGLL MEYLQRIPKP GEEVQVGDYL LKTLQVESHR VQKVQIIPLR
KDGEMEYEV
//
