SECDF_BACSU
ID SECDF_BACSU Reviewed; 737 AA.
AC O32047;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1999, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Protein translocase subunit SecDF;
GN Name=secDF; OrderedLocusNames=BSU27650;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN PROTEIN SECRETION, TOPOLOGY,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=9694879; DOI=10.1074/jbc.273.33.21217;
RA Bolhuis A., Broekhuizen C.P., Sorokin A., van Roosmalen M.L., Venema G.,
RA Bron S., Quax W.J., van Dijl J.M.;
RT "SecDF of Bacillus subtilis, a molecular Siamese twin required for the
RT efficient secretion of proteins.";
RL J. Biol. Chem. 273:21217-21224(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SUBUNIT.
RX PubMed=11524133; DOI=10.1111/j.1574-6976.2001.tb00586.x;
RA van Wely K.H.M., Swaving J., Freudl R., Driessen A.J.M.;
RT "Translocation of proteins across the cell envelope of Gram-positive
RT bacteria.";
RL FEMS Microbiol. Rev. 25:437-454(2001).
RN [4]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / PY79;
RX PubMed=15995216; DOI=10.1128/jb.187.14.5000-5002.2005;
RA Rubio A., Jiang X., Pogliano K.;
RT "Localization of translocation complex components in Bacillus subtilis:
RT enrichment of the signal recognition particle receptor at early sporulation
RT septa.";
RL J. Bacteriol. 187:5000-5002(2005).
CC -!- FUNCTION: Required for efficient translocation of secretory pre-
CC proteins under conditions of hypersecretion but is not required for the
CC release of mature proteins from the membrane.
CC {ECO:0000269|PubMed:9694879}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of the essential Sec protein translocation apparatus
CC which comprises SecA, SecYEG and auxiliary protein SecDF. Other
CC proteins may also be involved (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15995216};
CC Multi-pass membrane protein {ECO:0000269|PubMed:15995216}. Note=Found
CC uniformly distributed in both the mother cell and forespore following
CC sporulation.
CC -!- INDUCTION: Shows maximal expression at the beginning of post-
CC exponential growth phase and increased expression by glucose in the
CC post-exponential growth phase when cells are cultured on rich medium.
CC Expressed constitutively during growth in minimal medium.
CC {ECO:0000269|PubMed:9694879}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a cold-sensitive
CC phenotype and a filamentous morphology. {ECO:0000269|PubMed:9694879}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the SecD/SecF family.
CC SecD subfamily. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the SecD/SecF family.
CC SecF subfamily. {ECO:0000305}.
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DR EMBL; AF024506; AAC31122.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14724.2; -; Genomic_DNA.
DR PIR; H69704; H69704.
DR RefSeq; NP_390643.1; NC_000964.3.
DR RefSeq; WP_003245970.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O32047; -.
DR SMR; O32047; -.
DR STRING; 224308.BSU27650; -.
DR TCDB; 2.A.6.4.2; the resistance-nodulation-cell division (rnd) superfamily.
DR TCDB; 3.A.5.2.1; the general secretory pathway (sec) family.
DR jPOST; O32047; -.
DR PaxDb; O32047; -.
DR PRIDE; O32047; -.
DR EnsemblBacteria; CAB14724; CAB14724; BSU_27650.
DR GeneID; 937938; -.
DR KEGG; bsu:BSU27650; -.
DR PATRIC; fig|224308.179.peg.3004; -.
DR eggNOG; COG0341; Bacteria.
DR eggNOG; COG0342; Bacteria.
DR InParanoid; O32047; -.
DR OMA; RTVNTGM; -.
DR PhylomeDB; O32047; -.
DR BioCyc; BSUB:BSU27650-MON; -.
DR Proteomes; UP000001570; 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:0015031; P:protein transport; IBA:GO_Central.
DR GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01463_B; SecD_B; 1.
DR HAMAP; MF_01464_B; SecF_B; 1.
DR InterPro; IPR005791; SecD.
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; 2.
DR Pfam; PF07549; Sec_GG; 1.
DR Pfam; PF02355; SecD_SecF; 2.
DR PRINTS; PR01755; SECFTRNLCASE.
DR TIGRFAMs; TIGR00916; 2A0604s01; 2.
DR TIGRFAMs; TIGR00966; 3a0501s07; 1.
DR TIGRFAMs; TIGR01129; secD; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..737
FT /note="Protein translocase subunit SecDF"
FT /id="PRO_0000384402"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9694879"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..254
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:9694879"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9694879"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..301
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:9694879"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9694879"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..380
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:9694879"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 402..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9694879"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 475..569
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:9694879"
FT TRANSMEM 570..590
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 591..593
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9694879"
FT TRANSMEM 594..614
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 615..621
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:9694879"
FT TRANSMEM 622..642
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 643..677
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9694879"
FT TRANSMEM 678..698
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 699
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:9694879"
FT TRANSMEM 700..720
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 721..737
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9694879"
FT REGION 1..416
FT /note="SecD"
FT REGION 446..737
FT /note="SecF"
SQ SEQUENCE 737 AA; 81654 MW; 54C397E939779177 CRC64;
MKKGRLIAFF LFVLLIGTGL GYFTKPAANN ITLGLDLQGG FEVLYDVQPV KKGDKITKDV
LVSTVEALNR RANVLGVSEP NIQIEGNNRI RVQLAGVTNQ NRAREILATE AQLSFRDAND
KELLNGADLV ENGAKQTYDS TTNEPIVTIK LKDADKFGEV TKKVMKMAPN NQLVIWLDYD
KGDSFKKEVQ KEHPKFVSAP NVSQELNTTD VKIEGHFTAQ EAKDLASILN AGALPVKLTE
KYSTSVGAQF GQQALHDTVF AGIVGIAIIF LFMLFYYRLP GLIAVITLSV YIYITLQIFD
WMNAVLTLPG IAALILGVGM AVDANIITYE RIKEELKLGK SVRSAFRSGN RRSFATIFDA
NITTIIAAVV LFIFGTSSVK GFATMLILSI LTSFITAVFL SRFLLALLVE SRWLDRKKGW
FGVNKKHIMD IQDTDENTEP HTPFQKWDFT SKRKYFFIFS SAVTVAGIII LLVFRLNLGI
DFASGARIEV QSDHKLTTEQ VEKDFESLGM DPDTVVLSGE KSNIGVARFV GVPDKETIAK
VKTYFKDKYG SDPNVSTVSP TVGKELARNA LYAVAIASIG IIIYVSIRFE YKMAIAAIAS
LLYDAFFIVT FFSITRLEVD VTFIAAILTI IGYSINDTIV TFDRVREHMK KRKPKTFADL
NHIVNLSLQQ TFTRSINTVL TVVIVVVTLL IFGASSITNF SIALLVGLLT GVYSSLYIAA
QIWLAWKGRE LKKDSAQ
