ID I2ETV3_EMTOG Unreviewed; 1000 AA. AC I2ETV3; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 10-MAY-2017, entry version 32. DE RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463}; DE AltName: Full=Protein-export membrane protein SecF {ECO:0000256|HAMAP-Rule:MF_01464}; GN Name=secD {ECO:0000256|HAMAP-Rule:MF_01463}; GN Synonyms=secF {ECO:0000256|HAMAP-Rule:MF_01464}; GN OrderedLocusNames=Emtol_1966 {ECO:0000313|EMBL:AFK03106.1}; OS Emticicia oligotrophica (strain DSM 17448 / GPTSA100-15). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Emticicia. OX NCBI_TaxID=929562 {ECO:0000313|EMBL:AFK03106.1, ECO:0000313|Proteomes:UP000002875}; RN [1] {ECO:0000313|EMBL:AFK03106.1, ECO:0000313|Proteomes:UP000002875} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17448 / GPTSA100-15 {ECO:0000313|Proteomes:UP000002875}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., RA Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., RA Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of chromosome of Emticicia oligotrophica DSM RT 17448."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Part of the Sec protein translocase complex. Interacts CC with the SecYEG preprotein conducting channel. SecDF uses the CC proton motive force (PMF) to complete protein translocation after CC the ATP-dependent function of SecA. {ECO:0000256|HAMAP- CC Rule:MF_01464, ECO:0000256|SAAS:SAAS00541769}. CC -!- SUBUNIT: Forms a complex with SecD. Part of the essential Sec CC protein translocation apparatus which comprises SecA, SecYEG and CC auxiliary 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 CC protein translocation apparatus which comprises SecA, SecYEG and CC auxiliary proteins SecDF. Other proteins may also be involved. CC {ECO:0000256|HAMAP-Rule:MF_01463}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_01464}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01464}. 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 CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01464}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP002961; AFK03106.1; -; Genomic_DNA. DR RefSeq; WP_015028804.1; NC_018748.1. DR RefSeq; WP_015028804.1; NC_018748.1. DR RefSeq; WP_015028804.1; NC_018748.1. DR EnsemblBacteria; AFK03106; AFK03106; Emtol_1966. DR KEGG; eol:Emtol_1966; -. DR KO; K12257; -. DR OMA; GVTQPNI; -. DR OrthoDB; POG091H02C5; -. DR BioCyc; EOLI929562:GLCO-1641-MONOMER; -. DR Proteomes; UP000002875; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015450; F:P-P-bond-hydrolysis-driven protein transmembrane transporter activity; IEA:InterPro. DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-HAMAP. DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-HAMAP. DR GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-HAMAP. 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 Pfam; PF07549; Sec_GG; 2. DR Pfam; PF02355; SecD_SecF; 2. DR PRINTS; PR01755; SECFTRNLCASE. DR TIGRFAMs; TIGR00916; 2A0604s01; 1. DR TIGRFAMs; TIGR00966; 3a0501s07; 1. DR TIGRFAMs; TIGR01129; secD; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01464}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01464, KW ECO:0000256|SAAS:SAAS00425060}; KW Complete proteome {ECO:0000313|Proteomes:UP000002875}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01464, KW ECO:0000256|SAAS:SAAS00284057}; KW Protein transport {ECO:0000256|HAMAP-Rule:MF_01464, KW ECO:0000256|SAAS:SAAS00425133}; KW Reference proteome {ECO:0000313|Proteomes:UP000002875}; KW Translocation {ECO:0000256|HAMAP-Rule:MF_01464, KW ECO:0000256|SAAS:SAAS00425069}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01464, KW ECO:0000256|SAAS:SAAS00425065}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01464, KW ECO:0000256|SAAS:SAAS00425143}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01464, KW ECO:0000256|SAAS:SAAS00425109}. FT TRANSMEM 504 524 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01464}. FT TRANSMEM 529 551 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01464}. FT TRANSMEM 557 576 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01464}. FT TRANSMEM 609 627 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01464}. FT TRANSMEM 633 652 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01464}. FT TRANSMEM 686 704 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01464}. FT TRANSMEM 807 828 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01464}. FT TRANSMEM 835 857 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01464}. FT TRANSMEM 869 890 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01464}. FT TRANSMEM 923 941 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01464}. FT TRANSMEM 947 971 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01464}. SQ SEQUENCE 1000 AA; 107812 MW; 8F45E1E98117C726 CRC64; MRNKGGIVAL LVAFLAISVY FLARTWKAND IRKDAEAYAT DKSGKVDYTK KQRYLDSLWK QPVFLGMTTT EDLMKQELGL GLDLQGGMSV ILEVSPTEIV RALANSRDPK VATAISKAQE RAANSSANFV DLFAEEFKKV APDTKLSSIF SNSSNRGTLS LESSDSQVIS YIKKEVDGAF DRAFRIIQTR VDKFGVANPN LQRLSGTNRI QVELPGVDNP QRVRKLLSGA AKLEFCEVYS MQEIAPAFDG LSAILLQMDA EAKAAAKTDL NKIAGKGDNA AAATNDTSKN SLAAKLAGGS KTDTSKKDST ALAQRQSNAF SNLFVGTGYG VAVRVKDTSR VNQIMRRPDV QSLFPADANF VYDVKPRANG TNANEDIVDI YFVKDLGKAP LEGDVVTNAT QDFDERGKPA VEMQMNAEGA RKWKALTAAN VGRQVAIILD NFVYSAPVVN GEIGGGRSSI SGNFTVEEAL DLANVLKAGK LPAPTNVISE DIVGATVGSE AARAGILSSI IGVLFVLAFV MIYYNKAGLI ANIALIVNLF LLLGVMASFG ATLTLPGIAG LVLSVGMSVD ANVLIYERIK EELALGKTFA TAVRDGFQNA MSSIIDSNVT TLITGAVLFI FGSGLILGFA TTLLIGIFTS LFSAIFVSRL LFEYYIGKGK TVSFYTKFTE KLFKDSQFDF VSKRKLYYTI SSAIIIAGIV SIFFKGFGLG VDFLGGRTYV AKFEKTVNTE EIDAALKGTF EGQAIEVKTF GGFDQVKITT PYKIENTNPE IEKQIENNVN NALANVNGNK GKITSSSKVG PTIANDAIGG ALKAILLSIA LVFIYIYLRF RSLAFGYGAL VALFHDVAII LGIFSIFRGW LPFSLDVDQA FVGAVLTIMG YSMNDTVVVF DRVREYLREK RGVREDIPTV INNALNSTLS RTAVTGFSTL IVLLVLLIFG GETIRGFVFA MFVGVIVGTY SSLFVATPIV VDAMQRDLKN EDAKLAAVPV DAEAKKGKKA //