SECF_THET1
ID SECF_THET1 Reviewed; 317 AA.
AC D1CDJ6;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Protein translocase subunit SecF;
GN Name=secF {ECO:0000255|HAMAP-Rule:MF_01464}; OrderedLocusNames=Tter_0080;
OS Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC Bacteria; Chloroflexi; Thermobaculum.
OX NCBI_TaxID=525904;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-798 / YNP1;
RX DOI=10.4056/sigs.1153107;
RA Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T., Nolan M.,
RA Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y., Jeffries C., Lu M., Brettin T., Detter J., Goker M.,
RA Tindall B., Beck B., McDermott T., Woyke T., Bristow J., Eisen J.,
RA Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Cheng J.;
RT "Complete genome sequence of Thermobaculum terrenum type strain (YNP1T).";
RL Stand. Genomic Sci. 3:153-162(2010).
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:0000255|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:0000255|HAMAP-Rule:MF_01464}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01464};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01464}.
CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01464}.
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DR EMBL; CP001825; ACZ41002.1; -; Genomic_DNA.
DR RefSeq; WP_012874037.1; NC_013525.1.
DR AlphaFoldDB; D1CDJ6; -.
DR SMR; D1CDJ6; -.
DR STRING; 525904.Tter_0080; -.
DR EnsemblBacteria; ACZ41002; ACZ41002; Tter_0080.
DR KEGG; ttr:Tter_0080; -.
DR eggNOG; COG0341; Bacteria.
DR HOGENOM; CLU_050012_0_0_0; -.
DR OMA; AFEWRMA; -.
DR OrthoDB; 410730at2; -.
DR Proteomes; UP000000323; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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; IPR005665; SecF_bac.
DR PANTHER; PTHR30081; PTHR30081; 1.
DR Pfam; PF07549; Sec_GG; 1.
DR Pfam; PF02355; SecD_SecF; 1.
DR PRINTS; PR01755; SECFTRNLCASE.
DR TIGRFAMs; TIGR00966; 3a0501s07; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..317
FT /note="Protein translocase subunit SecF"
FT /id="PRO_0000412704"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 244..266
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 276..298
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
SQ SEQUENCE 317 AA; 35531 MW; C255EC102EF66537 CRC64;
MIDIVRWRYA FYLLSLLIII PGTIYLLLFG LRLGIDFEGG TFWQIQFEKP VRIEDVRSAL
AQAGYNEAFV QSFGQQSNTA QGTVTRGVSM RLPEIKENSP EKAKLEQILK SRFGNYEELV
FTSVGPAVGR EIRNRSIVAI ALASLGILGY IAFAFRKVSH PFRYGICAII AMLHDVLVVV
GIFAILGKHF GVEIDALFVT ALLTVIGFSV HDTIVVFDRI RENQLRRYGE SFEQIVNISL
LQTLVRSVNT SMTVIFTLLA LYFFGGTTIK HFVLALLIGI VSGTYSSIFN ASLLLVSWEN
KDFLRIFRRT EPEAAAT