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Database: UniProt
Entry: C4L7L1_TOLAT
LinkDB: C4L7L1_TOLAT
Original site: C4L7L1_TOLAT 
ID   C4L7L1_TOLAT            Unreviewed;       617 AA.
AC   C4L7L1;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   OrderedLocusNames=Tola_2028 {ECO:0000313|EMBL:ACQ93627.1};
OS   Tolumonas auensis (strain DSM 9187 / TA4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Tolumonas.
OX   NCBI_TaxID=595494 {ECO:0000313|EMBL:ACQ93627.1, ECO:0000313|Proteomes:UP000009073};
RN   [1] {ECO:0000313|Proteomes:UP000009073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9187 / TA4 {ECO:0000313|Proteomes:UP000009073};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Spring S.,
RA   Beller H.;
RT   "Complete sequence of Tolumonas auensis DSM 9187.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACQ93627.1, ECO:0000313|Proteomes:UP000009073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9187 / TA4 {ECO:0000313|Proteomes:UP000009073};
RX   PubMed=22180815; DOI=10.4056/sigs.2184986;
RA   Chertkov O., Copeland A., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA   Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Richardson P.,
RA   Bruce D., Goodwin L., Han C., Tapia R., Saunders E., Schmutz J.,
RA   Brettin T., Larimer F., Land M., Hauser L., Spring S., Rohde M.,
RA   Kyrpides N.C., Ivanova N., Goker M., Beller H.R., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of Tolumonas auensis type strain (TA 4).";
RL   Stand. Genomic Sci. 5:112-120(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:0000256|HAMAP-Rule:MF_01463}.
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-YajC and YidC. {ECO:0000256|HAMAP-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}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC       membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01463}.
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DR   EMBL; CP001616; ACQ93627.1; -; Genomic_DNA.
DR   RefSeq; WP_015879095.1; NC_012691.1.
DR   AlphaFoldDB; C4L7L1; -.
DR   STRING; 595494.Tola_2028; -.
DR   KEGG; tau:Tola_2028; -.
DR   eggNOG; COG0342; Bacteria.
DR   HOGENOM; CLU_007894_4_3_6; -.
DR   OrthoDB; 9805019at2; -.
DR   Proteomes; UP000009073; 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; 3.30.70.260; -; 1.
DR   Gene3D; 3.30.70.3400; -; 2.
DR   Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 1.
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   InterPro; IPR048631; SecD_1st.
DR   InterPro; IPR048634; SecD_SecF_C.
DR   NCBIfam; TIGR00916; 2A0604s01; 1.
DR   NCBIfam; TIGR01129; secD; 1.
DR   PANTHER; PTHR30081:SF1; PROTEIN TRANSLOCASE SUBUNIT SECD; 1.
DR   PANTHER; PTHR30081; PROTEIN-EXPORT MEMBRANE PROTEIN SEC; 1.
DR   Pfam; PF07549; Sec_GG; 1.
DR   Pfam; PF13721; SecD-TM1; 1.
DR   Pfam; PF21760; SecD_1st; 1.
DR   Pfam; PF02355; SecD_SecF; 1.
DR   SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01463};
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}; Reference proteome {ECO:0000313|Proteomes:UP000009073};
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        7..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        455..474
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        481..502
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        508..530
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        551..573
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        579..603
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   DOMAIN          2..103
FT                   /note="SecD export protein N-terminal TM"
FT                   /evidence="ECO:0000259|Pfam:PF13721"
FT   DOMAIN          229..288
FT                   /note="Protein translocase subunit SecDF P1"
FT                   /evidence="ECO:0000259|Pfam:PF21760"
FT   DOMAIN          435..601
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
SQ   SEQUENCE   617 AA;  67061 MW;  C81948DC76228A00 CRC64;
     MLNRYPLWKY LMVAFVVIIG TLYSAPNLYG EDPALQVSAI RGHDVKVDTL DTVKKSLDTA
     KISIKSAVLE NNQILVRFNN TDDQLQAREL VTQALGDKFI TALNLAPATP EWLTSIGASP
     LKLGLDLRGG VHFLMEVDMD EAINKAQEQL VQDFRTSLRE DGIRYAGVRR AAGDVVVAFR
     DSDTQQKGLA HLRKRHIDLT LTDYEDKGQF WVKASMSEAK QKSVTEDALE QNITIIRNRV
     NELGVAEPLV QRQGTARIVV ELPGIQDTAR AKEILGATAT LEFRLVDENA DAAAAMNGQV
     PPNSELFYDR NGRPVVLQKR IILTGDHITG SSSSADEYGR PQVSIKLDGV GGNRMSTATK
     DSIGKAMASV FIEYKPVGEP GADGKRRIEK HEEVINVATI QSRLGSDFRI TGIDTTQEAH
     NLSLLLRSGA LTAPIQIVEE RTIGPSMGQA NIDSGLSALG MGTLILVIFM AIYYKLFGVV
     ANIALMFNVV LMIGVMSMIP GATMTLPGIA GIVLTLGMAV DANVLIYERI REELRAGRGV
     QQAIHLGYER AFATIADSNI TTFITALILF AVGTGPVRGF ALVLMIGILC SMFTAITGSR
     AIVNLIWGGR KVKDLSI
//
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