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Database: UniProt
Entry: D7DM25_METV0
LinkDB: D7DM25_METV0
Original site: D7DM25_METV0 
ID   D7DM25_METV0            Unreviewed;       614 AA.
AC   D7DM25;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   OrderedLocusNames=M301_2356 {ECO:0000313|EMBL:ADI30719.1};
OS   Methylotenera versatilis (strain 301).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylotenera.
OX   NCBI_TaxID=666681 {ECO:0000313|EMBL:ADI30719.1, ECO:0000313|Proteomes:UP000000383};
RN   [1] {ECO:0000313|Proteomes:UP000000383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 {ECO:0000313|Proteomes:UP000000383};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Clum A., Land M., Hauser L., Kyrpides N., Ivanova N.,
RA   Chistoservova L., Kalyuzhnaya M., Woyke T.;
RT   "Complete sequence of Methylotenera sp. 301.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADI30719.1, ECO:0000313|Proteomes:UP000000383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 {ECO:0000313|EMBL:ADI30719.1,
RC   ECO:0000313|Proteomes:UP000000383};
RX   PubMed=21622745; DOI=10.1128/JB.00404-11;
RA   Lapidus A., Clum A., Labutti K., Kaluzhnaya M.G., Lim S., Beck D.A.,
RA   Glavina Del Rio T., Nolan M., Mavromatis K., Huntemann M., Lucas S.,
RA   Lidstrom M.E., Ivanova N., Chistoserdova L.;
RT   "Genomes of three methylotrophs from a single niche uncover genetic and
RT   metabolic divergence of Methylophilaceae.";
RL   J. Bacteriol. 193:3757-3764(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}.
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; CP002056; ADI30719.1; -; Genomic_DNA.
DR   RefSeq; WP_013149027.1; NC_014207.1.
DR   AlphaFoldDB; D7DM25; -.
DR   STRING; 666681.M301_2356; -.
DR   KEGG; meh:M301_2356; -.
DR   eggNOG; COG0342; Bacteria.
DR   HOGENOM; CLU_007894_4_3_4; -.
DR   OrthoDB; 9805019at2; -.
DR   Proteomes; UP000000383; 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; -; 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:UP000000383};
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        446..466
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        473..492
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        573..597
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   DOMAIN          1..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          427..595
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
SQ   SEQUENCE   614 AA;  66875 MW;  1EF8F9B9A4B33DA9 CRC64;
     MNRYPMWKNI LVAVMILIGL IYTIPNFFGE SPAVQITPAK STTKLDSALL DKVEDIFKQE
     KIEYDGVYQD ARGVKARFKN TDTQIRAKDV LQANLGTDYT VALNLLSRSP NWLRSLGAKP
     MYLGLDLRGG VHFLMQVDMK AALSKAAERF VGDFKIALRK ERISYVGVSR EGETVQIHFN
     NAEELTKAHA VIAKEYPNLT LEESTIGEEK ILKASLNLVE QKSIQDFAIK QNIQTLHNRI
     NELGVAEPII QQQGADRVVV QLPGVQDTAK AKEILGRTAT LEIRMVDEEK SDAATLEKAE
     KGQAPIGDDV FKNRDGRAVL VKKSVVLTGD YITDAGPGVD SQSGRSTVNV TLDARGARIF
     QQVTRENVGK RMAILLIEKG STEVITAPTI NEEIGGGRVQ ISGMANTQEA TDIALLLRAG
     ALAAPMDIVE ERTVGPSMGQ DNINRGIHST LWGFAAIAVM MMIYYVAFGA VSVTALAINL
     LLLVAILSML QATLTLPGLA AIALALGMAI DANVLINERI REELRNGNTP QASIHAGYER
     AWDTILDSNV TTLIAGLALF MFGTGPIKGF AVVHVLGILT SMFSAVLVSR AIVNLIYGYR
     RKLTKLSIGQ IYKG
//
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