SECF_MYCTU
ID SECF_MYCTU Reviewed; 442 AA.
AC P9WGN9; L0TD04; Q50635;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Protein translocase subunit SecF;
GN Name=secF {ECO:0000255|HAMAP-Rule:MF_01464}; OrderedLocusNames=Rv2586c;
GN ORFNames=MTCY227.15;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(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: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; AL123456; CCP45382.1; -; Genomic_DNA.
DR PIR; A70726; A70726.
DR RefSeq; NP_217102.1; NC_000962.3.
DR RefSeq; WP_003899387.1; NZ_NVQJ01000023.1.
DR AlphaFoldDB; P9WGN9; -.
DR SMR; P9WGN9; -.
DR STRING; 83332.Rv2586c; -.
DR PaxDb; P9WGN9; -.
DR DNASU; 887229; -.
DR GeneID; 887229; -.
DR KEGG; mtu:Rv2586c; -.
DR TubercuList; Rv2586c; -.
DR eggNOG; COG0341; Bacteria.
DR OMA; AFEWRMA; -.
DR PhylomeDB; P9WGN9; -.
DR Reactome; R-HSA-1222387; Tolerance of reactive oxygen produced by macrophages.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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:0015031; P:protein transport; IBA:GO_Central.
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; TIGR00916; 2A0604s01; 1.
DR TIGRFAMs; TIGR00966; 3a0501s07; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..442
FT /note="Protein translocase subunit SecF"
FT /id="PRO_0000095983"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 442 AA; 47014 MW; 09427E2AD59CD6FA CRC64;
MASKAKTGRD DEATSAVELT EATESAVART DGDSTTDTAS KLGHHSFLSR LYTGTGAFEV
VGRRRLWFGV SGAIVAVAIA SIVFRGFTFG IDFKGGTTVS FPRGSTQVAQ VEDVYYRALG
SEPQSVVIVG AGASATVQIR SETLTSDQTA KLRDALFEAF GPKGTDGQPS KQAISDSAVS
ETWGGQITKK AVIALVVFLV LVALYITVRY ERYMTISAIT AMLFDLTVTA GVYSLVGFEV
TPATVIGLLT ILGFSLYDTV IVFDKVEENT HGFQHTTRRT FAEQANLAIN QTFMRSINTS
LIGVLPVLAL MVVAVWLLGV GTLKDLALVQ LIGIIIGTYS SIFFATPLLV TLRERTELVR
NHTRRVLKRR NSGSPAGSED ASTDGGEQPA AADEQSLVGI TQASSQSAPR AAQGSSKPAP
GARPVRPVGT RRPTGKRNAG RR
