ID H9ZSD9_THETH Unreviewed; 735 AA.
AC H9ZSD9;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_01463, ECO:0000256|HAMAP-Rule:MF_01464};
DE Includes:
DE RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
DE Includes:
DE RecName: Full=Protein-export membrane protein SecF {ECO:0000256|HAMAP-Rule:MF_01464};
GN Name=secF {ECO:0000256|HAMAP-Rule:MF_01464};
GN Synonyms=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN ORFNames=TtJL18_1365 {ECO:0000313|EMBL:AFH39249.1};
OS Thermus thermophilus JL-18.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=798128 {ECO:0000313|EMBL:AFH39249.1, ECO:0000313|Proteomes:UP000007388};
RN [1] {ECO:0000313|EMBL:AFH39249.1, ECO:0000313|Proteomes:UP000007388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JL-18 {ECO:0000313|EMBL:AFH39249.1,
RC ECO:0000313|Proteomes:UP000007388};
RX PubMed=23405355; DOI=10.1128/genomeA.00106-12;
RA Murugapiran S.K., Huntemann M., Wei C.L., Han J., Detter J.C., Han C.S.,
RA Erkkila T.H., Teshima H., Chen A., Kyrpides N., Mavrommatis K.,
RA Markowitz V., Szeto E., Ivanova N., Pagani I., Lam J., McDonald A.I.,
RA Dodsworth J.A., Pati A., Goodwin L., Peters L., Pitluck S., Woyke T.,
RA Hedlund B.P.;
RT "Whole Genome Sequencing of Thermus oshimai JL-2 and Thermus thermophilus
RT JL-18, Incomplete Denitrifiers from the United States Great Basin.";
RL Genome Announc. 1:E00106-E00112(2013).
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_01463}.
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 -!- SUBUNIT: Forms a complex with SecF. 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_01463}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01463};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01463}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01463}.
CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01464}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01463}.
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DR EMBL; CP003252; AFH39249.1; -; Genomic_DNA.
DR RefSeq; WP_014629864.1; NC_017587.1.
DR AlphaFoldDB; H9ZSD9; -.
DR STRING; 798128.TtJL18_1365; -.
DR KEGG; ttl:TtJL18_1365; -.
DR PATRIC; fig|798128.4.peg.1332; -.
DR HOGENOM; CLU_007894_3_2_0; -.
DR Proteomes; UP000007388; 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; 3.30.1360.200; -; 1.
DR Gene3D; 3.30.70.3400; -; 1.
DR Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 2.
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; IPR048631; SecD_1st.
DR InterPro; IPR048634; SecD_SecF_C.
DR InterPro; IPR005665; SecF_bac.
DR InterPro; IPR000731; SSD.
DR NCBIfam; TIGR00916; 2A0604s01; 2.
DR NCBIfam; TIGR01129; secD; 1.
DR NCBIfam; TIGR00966; transloc_SecF; 1.
DR PANTHER; PTHR30081:SF1; PROTEIN TRANSLOCASE SUBUNIT SECD; 1.
DR PANTHER; PTHR30081; PROTEIN-EXPORT MEMBRANE PROTEIN SEC; 1.
DR Pfam; PF07549; Sec_GG; 2.
DR Pfam; PF21760; SecD_1st; 1.
DR Pfam; PF02355; SecD_SecF; 2.
DR PRINTS; PR01755; SECFTRNLCASE.
DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR PROSITE; PS50156; SSD; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01463};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01463};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW Rule:MF_01463};
KW Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW Rule:MF_01463};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01463};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01463};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01463}.
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 300..321
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 327..346
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 367..392
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 398..417
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 450..468
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 570..587
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 594..615
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 621..641
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 673..691
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 697..723
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 591..722
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
SQ SEQUENCE 735 AA; 79513 MW; 324DF7DD8B904596 CRC64;
MNRKNLTSLF LLGVFLLALL FVWKPWAPEE PKVRLGLDLK GGLRIVLEAD VENPTLDDLE
KARTVLENRI NALGVAEPLI QIQGQKRIVV ELPGLSQADQ DRALKLIGQR AVLEFRIVKE
GATGTTVAQI NQALRENPRL NREELEKDLI KPEDLGPPLL TGADLADARA VFDQFGRPQV
SLTFTPEGAK KFEEVTRQNI GKRLAIVLDG RVYTAPVIRQ AITGGQAVIE GLSSVEEASE
IALVLRSGSL PVPLKVAEIR AIGPTLGQDA IQAGIRSALI GTLAIFLLIF AYYGPHLGLV
ASLGLIYTSA LILGLLSGLG ATLTLPGIAG LVLTLGAAVD GNVLSFERIK EELRAGKKLR
QAIPEGFRHS TLTIMDVNIA HLLAAAALYQ YATGPVRGFA VILAIGVVAS VFSNLVFSRH
LLERLADRGE IRPPMWLVDP RFNFMGPARY ITAATLLLAA LAAGVALTKG FNYSIDFTGG
TAYTLRTEPE AGVDTLRRFL EEKGFPAKEA VITQVQAPTA AYREFLVKLP PLSDERRLEL
ERLLASELKA TVLASETVGP AIGEELRRNA VMAVLVGLGL ILLYVAFRFD WTFGVASILA
VAHDVAIVAG MYSLLGLEFS IPTIAALLTI VGYSINDSIV VSDRIRENQK LLRHLPYAEL
VNRSINQTLS RTVMTSLTTL LPILALLFLG GSVLRDFALA IFVGIFVGTY SSIYVVSALV
VAWKNRGKAQ EAKKA
//
