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Database: UniProt
Entry: E4Q4C3_CALOW
LinkDB: E4Q4C3_CALOW
Original site: E4Q4C3_CALOW 
ID   E4Q4C3_CALOW            Unreviewed;       310 AA.
AC   E4Q4C3;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=Protein-export membrane protein SecF {ECO:0000256|HAMAP-Rule:MF_01464};
GN   Name=secF {ECO:0000256|HAMAP-Rule:MF_01464};
GN   OrderedLocusNames=Calow_0502 {ECO:0000313|EMBL:ADQ04085.1};
OS   Caldicellulosiruptor owensensis (strain ATCC 700167 / DSM 13100 / OL).
OC   Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC   Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX   NCBI_TaxID=632518 {ECO:0000313|EMBL:ADQ04085.1, ECO:0000313|Proteomes:UP000006889};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OL;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA   Mikhailova N., Blumer-Schuette S.E., Kelly R.M., Woyke T.;
RT   "Complete sequence of Caldicellulosiruptor owensensis OL.";
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADQ04085.1, ECO:0000313|Proteomes:UP000006889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700167 / DSM 13100 / OL
RC   {ECO:0000313|Proteomes:UP000006889};
RX   PubMed=21216991; DOI=10.1128/JB.01515-10;
RA   Blumer-Schuette S.E., Ozdemir I., Mistry D., Lucas S., Lapidus A.,
RA   Cheng J.F., Goodwin L.A., Pitluck S., Land M.L., Hauser L.J., Woyke T.,
RA   Mikhailova N., Pati A., Kyrpides N.C., Ivanova N., Detter J.C.,
RA   Walston-Davenport K., Han S., Adams M.W., Kelly R.M.;
RT   "Complete genome sequences for the anaerobic, extremely thermophilic plant
RT   biomass-degrading bacteria Caldicellulosiruptor hydrothermalis,
RT   Caldicellulosiruptor kristjanssonii, Caldicellulosiruptor kronotskyensis,
RT   Caldicellulosiruptor owensenis, and Caldicellulosiruptor lactoaceticus.";
RL   J. Bacteriol. 193:1483-1484(2011).
CC   -!- FUNCTION: Part of the Sec protein translocase complex. Interacts with
CC       the SecYEG preprotein conducting channel. SecDF uses the proton motive
CC       force (PMF) to complete protein translocation after the ATP-dependent
CC       function of SecA. {ECO:0000256|HAMAP-Rule:MF_01464}.
CC   -!- SUBUNIT: Forms a complex with SecD. Part of the essential Sec protein
CC       translocation apparatus which comprises SecA, SecYEG and auxiliary
CC       proteins SecDF. Other proteins may also be involved.
CC       {ECO:0000256|HAMAP-Rule:MF_01464}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01464};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01464}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01464}.
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DR   EMBL; CP002216; ADQ04085.1; -; Genomic_DNA.
DR   RefSeq; WP_013411495.1; NC_014657.1.
DR   AlphaFoldDB; E4Q4C3; -.
DR   STRING; 632518.Calow_0502; -.
DR   KEGG; cow:Calow_0502; -.
DR   eggNOG; COG0341; Bacteria.
DR   HOGENOM; CLU_050012_0_0_9; -.
DR   OMA; AFEWRMA; -.
DR   OrthoDB; 9805019at2; -.
DR   Proteomes; UP000006889; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015450; F:protein-transporting ATPase activity; IEA:InterPro.
DR   GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule.
DR   GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 1.
DR   HAMAP; MF_01464_B; SecF_B; 1.
DR   InterPro; IPR022813; SecD/SecF_arch_bac.
DR   InterPro; IPR022645; SecD/SecF_bac.
DR   InterPro; IPR022646; SecD/SecF_CS.
DR   InterPro; IPR048634; SecD_SecF_C.
DR   InterPro; IPR005665; SecF_bac.
DR   NCBIfam; TIGR00916; 2A0604s01; 1.
DR   NCBIfam; TIGR00966; transloc_SecF; 1.
DR   PANTHER; PTHR30081:SF8; PROTEIN TRANSLOCASE SUBUNIT SECF; 1.
DR   PANTHER; PTHR30081; PROTEIN-EXPORT MEMBRANE PROTEIN SEC; 1.
DR   Pfam; PF07549; Sec_GG; 1.
DR   Pfam; PF02355; SecD_SecF; 1.
DR   PRINTS; PR01755; SECFTRNLCASE.
DR   SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_01464};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01464};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW   Rule:MF_01464}; Reference proteome {ECO:0000313|Proteomes:UP000006889};
KW   Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW   Rule:MF_01464};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01464};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01464};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01464}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        141..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        165..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        192..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        244..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        268..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   DOMAIN          120..295
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
SQ   SEQUENCE   310 AA;  34969 MW;  43F392C74BB025E6 CRC64;
     MTRIDFIGKR KYFYIVSILV MVIGLISYLV QGFNYDIDFT GGTVLEINLH KVPTAKEISE
     LEKLTKQITG TQTPIVRKVE DGKKIMINAH EVHGKKKTEL SKQTRDKLFA EIAKRYNLKK
     EDLVSYQNVG AVVSSELKSQ AIWAVVIASI LMLIYIAIRF EFRFGTTAVA ALIHDLLIVL
     TVYTLFRIPL NSTFIAAVLT VLGYSINDTI VVFDRIRENR RIAGKMELKD LVNLSMNQTI
     GRSIATAISV IIVLVVLYIM GVQSIKEFAF PLLIGVISGT YSSIFIATAL WFDWELSTRK
     KKLQAKPKRA
//
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