(data stored in SCRATCH zone)

SWISSPROT: Q145I2_PARXL

ID   Q145I2_PARXL            Unreviewed;       695 AA.
AC   Q145I2;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 82.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   ORFNames=Bxe_A3992 {ECO:0000313|EMBL:ABE29007.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE29007.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE29007.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE29007.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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_01463, ECO:0000256|SAAS:SAAS01082309}.
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-YajC and YidC. {ECO:0000256|HAMAP-
CC       Rule:MF_01463}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01463}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01463}.
CC   -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01463}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01463}.
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DR   EMBL; CP000270; ABE29007.1; -; Genomic_DNA.
DR   RefSeq; WP_011486830.1; NZ_CP008760.1.
DR   STRING; 266265.Bxe_A3992; -.
DR   EnsemblBacteria; ABE29007; ABE29007; Bxe_A3992.
DR   GeneID; 4002083; -.
DR   KEGG; bxb:DR64_1669; -.
DR   KEGG; bxe:Bxe_A3992; -.
DR   PATRIC; fig|266265.5.peg.495; -.
DR   eggNOG; ENOG4107QN8; Bacteria.
DR   eggNOG; COG0342; LUCA.
DR   HOGENOM; HOG000018637; -.
DR   KO; K03072; -.
DR   OMA; AAPMEII; -.
DR   OrthoDB; 121331at2; -.
DR   BioCyc; BXEN266265:BXE_RS02350-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 1.
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:P-P-bond-hydrolysis-driven protein transmembrane transporter 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_01463_B; SecD_B; 1.
DR   InterPro; IPR005791; SecD.
DR   InterPro; IPR027398; SecD-TM.
DR   InterPro; IPR022813; SecD/SecF_arch_bac.
DR   InterPro; IPR022645; SecD/SecF_bac.
DR   InterPro; IPR022646; SecD/SecF_CS.
DR   PANTHER; PTHR30081; PTHR30081; 1.
DR   Pfam; PF07549; Sec_GG; 1.
DR   Pfam; PF13721; SecD-TM1; 1.
DR   Pfam; PF02355; SecD_SecF; 1.
DR   TIGRFAMs; TIGR00916; 2A0604s01; 1.
DR   TIGRFAMs; TIGR01129; secD; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q145I2.
DR   SWISS-2DPAGE; Q145I2.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01463};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS01082273};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS01082292};
KW   Protein transport {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS01082319};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Translocation {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS01082267};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS01082280};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS01082333};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS01082300}.
FT   TRANSMEM    449    470       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    477    495       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    501    519       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    540    566       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    572    600       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   DOMAIN        1    112       SecD-TM1. {ECO:0000259|Pfam:PF13721}.
SQ   SEQUENCE   695 AA;  73433 MW;  CD00238D1C7760F5 CRC64;
     MNRYPLWKYA VMLVALVIGL VYTLPNLFGE APAVQVSSGK ATVKLDSTTL SAVEAALAAN
     QIKPDDVTFD NSATNANIRV RLPDTDTQLR VKDLLQKSLN SDPSDPQYIV ALNLQSASPR
     WLTALHALPM YLGLDLRGGV HFLLQVDMAG ALNKKLDSDA SDARTLLRDS NIRDGGVNRV
     NQTVVINFAD QATADIASKQ LGRSISELQW ASQTGPDGGV QLVGTFTPTV QKAVQDAALK
     QNITTLHNRV NELGVAEPVI QQQGSDRIVV ELPGVQDTAK AKDIIGRTAT LEARLADPVN
     THPNPSDPVP PGDELFTQGN QTPVLLRKQI IFTGDRIIDA SAGFDEHQRP SVNIRLDSAG
     GRAVASVSRD NIGKPMAMVL FEKGKGEVLT VATIQSELGD RFQITGQATP QGAADLALLL
     RAGSLAAPMD IIEERTIGPS LGADNIRKGF HSVVWGFAAI AVFMIAYYML FGVISMIGLS
     VNLLLLIAVL SMLQATLTLP GIAAIALALG MAIDANVLIN ERVREELRNG APPQLAIQNG
     YAHAWATILD SNVTTLIAGI ALLAFGSGPV RGFAIVHCIG ILTSMFSAVF FSRGIVNLWY
     GGKKKLKSLA IGQVWRPDTA PAGSAAYLGS EDASTDTAQA VAAVAAKPSK ARAAVAQARA
     GKPTVRRRNA PGSSTGTPGS SPGSTNTPQK PGSSR
//

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