SECF_RICM5
ID SECF_RICM5 Reviewed; 308 AA.
AC A8F0L9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Protein translocase subunit SecF;
GN Name=secF {ECO:0000255|HAMAP-Rule:MF_01464}; OrderedLocusNames=RMA_0161;
OS Rickettsia massiliae (strain Mtu5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=416276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mtu5;
RX PubMed=17916642; DOI=10.1101/gr.6742107;
RA Blanc G., Ogata H., Robert C., Audic S., Claverie J.-M., Raoult D.;
RT "Lateral gene transfer between obligate intracellular bacteria: evidence
RT from the Rickettsia massiliae genome.";
RL Genome Res. 17:1657-1664(2007).
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-YajC and YidC. {ECO:0000255|HAMAP-Rule:MF_01464}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01464}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01464}.
CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01464}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABV84455.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000683; ABV84455.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_014013864.1; NC_009900.1.
DR AlphaFoldDB; A8F0L9; -.
DR SMR; A8F0L9; -.
DR EnsemblBacteria; ABV84455; ABV84455; RMA_0161.
DR GeneID; 57451873; -.
DR KEGG; rms:RMA_0161; -.
DR HOGENOM; CLU_050012_1_1_5; -.
DR Proteomes; UP000001311; Chromosome.
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 InterPro; IPR000731; SSD.
DR PANTHER; PTHR30081; PTHR30081; 1.
DR Pfam; PF07549; Sec_GG; 1.
DR Pfam; PF02355; SecD_SecF; 1.
DR PRINTS; PR01755; SECFTRNLCASE.
DR TIGRFAMs; TIGR00916; 2A0604s01; 1.
DR TIGRFAMs; TIGR00966; 3a0501s07; 1.
DR PROSITE; PS50156; SSD; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..308
FT /note="Protein translocase subunit SecF"
FT /id="PRO_0000316282"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
SQ SEQUENCE 308 AA; 34986 MW; CF6D08313C8BE3D1 CRC64;
MQIYPLRLLP NKIDFDFMNF KKVSYTFSII LSLISFIWIG IYKFNFGIDF AGGIVIEVRL
DQAPDLPKMR GVLGKLGIGE VVLQNFGSER DLSIRFGSSS EENLMKNIEL IKASLQSNFP
YKFEYRKVDF VGPQVGRQLI EAGAMAMLFS FLAIMVYIWV RFEWYFGLGI LIALVHDVIL
ALGFMSMTKL DFNLSTIAAV LTIIGYSVND SVVIYDRIRE NLRKYHKKNI TEIINLSINE
TLSRTILTVI TTLLANLALI LFGGEAIRSF SVLVFFGIIA GTYSSIFISA PILTMFVNRK
FNKKVIER