SECD_THET1
ID SECD_THET1 Reviewed; 515 AA.
AC D1CDJ5;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000255|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000255|HAMAP-Rule:MF_01463}; OrderedLocusNames=Tter_0079;
OS Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC Bacteria; Chloroflexi; Thermobaculum.
OX NCBI_TaxID=525904;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-798 / YNP1;
RX DOI=10.4056/sigs.1153107;
RA Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T., Nolan M.,
RA Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y., Jeffries C., Lu M., Brettin T., Detter J., Goker M.,
RA Tindall B., Beck B., McDermott T., Woyke T., Bristow J., Eisen J.,
RA Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Cheng J.;
RT "Complete genome sequence of Thermobaculum terrenum type strain (YNP1T).";
RL Stand. Genomic Sci. 3:153-162(2010).
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:0000255|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. Other proteins may also be involved.
CC {ECO:0000255|HAMAP-Rule:MF_01463}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01463};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01463}.
CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01463}.
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DR EMBL; CP001825; ACZ41001.1; -; Genomic_DNA.
DR RefSeq; WP_012874036.1; NC_013525.1.
DR AlphaFoldDB; D1CDJ5; -.
DR SMR; D1CDJ5; -.
DR STRING; 525904.Tter_0079; -.
DR EnsemblBacteria; ACZ41001; ACZ41001; Tter_0079.
DR KEGG; ttr:Tter_0079; -.
DR eggNOG; COG0342; Bacteria.
DR HOGENOM; CLU_007894_4_2_0; -.
DR OMA; MVVYYRL; -.
DR OrthoDB; 121331at2; -.
DR Proteomes; UP000000323; 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: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 HAMAP; MF_01463_B; SecD_B; 1.
DR InterPro; IPR001036; Acrflvin-R.
DR InterPro; IPR005791; SecD.
DR InterPro; IPR022813; SecD/SecF_arch_bac.
DR InterPro; IPR022645; SecD/SecF_bac.
DR PANTHER; PTHR30081; PTHR30081; 1.
DR Pfam; PF02355; SecD_SecF; 1.
DR PRINTS; PR00702; ACRIFLAVINRP.
DR TIGRFAMs; TIGR00916; 2A0604s01; 1.
DR TIGRFAMs; TIGR01129; secD; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..515
FT /note="Protein translocase subunit SecD"
FT /id="PRO_5000538081"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT REGION 141..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 515 AA; 55399 MW; 6532BC633321802E CRC64;
MRRSTLYSLI FIIILTAFAV WVDLPGSRNV FGRQAEVVEG LDLQGGLQVL LQARHVGGKA
PTREQMEEVR QVVEQRVNSL GLTEPVVQLQ GSDRIVVELP GVKDPEQAIR TFQGTGLLEF
IDAGDTPLQV GTLVNTTLGP AITNGNQNQN STKNGTPTPG TTPTPESTPQ ANQTPVAANV
TPTPEDPQFQ QALQATPPEQ LQRTYTTVIT GNDIANARPD FDPTTGEPVV SFELKPEAAK
KFADFTTQNV GKYLAIALDK KIISSPQIRD PITNGRGVIT GVTREEARTL AIQIRSGSLS
VPLDIISSNT VGATLGNDSV QRSIRAGLIG IGAVALFMIL YYRLPGFVSV VALAIYAAVV
FALFKLIPVT LTLAGIAGFI LSVGMAVDAN VLIFARLKDE LRRGRGLIQA IDVGFKNAWP
SIRDSNISTL ITCAILIWFG SRFGASVIKG FAITLAIGVI VSMFTAIFVT RTLLQVVLSM
VHTRNLWIWG IGKNQLPEPE GRTLQPAKSS RTTQA
