SECD_RHOM4
ID SECD_RHOM4 Reviewed; 622 AA.
AC D0MIN4;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, 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=Rmar_1455;
OS Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) (Rhodothermus
OS obamensis).
OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC Rhodothermaceae; Rhodothermus.
OX NCBI_TaxID=518766;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43812 / DSM 4252 / R-10;
RX PubMed=21304669; DOI=10.4056/sigs.46736;
RA Nolan M., Tindall B.J., Pomrenke H., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E.,
RA Han C., Bruce D., Goodwin L., Chain P., Pitluck S., Ovchinikova G.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Detter J.C.;
RT "Complete genome sequence of Rhodothermus marinus type strain (R-10).";
RL Stand. Genomic Sci. 1:283-291(2009).
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 inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01463}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC 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; CP001807; ACY48342.1; -; Genomic_DNA.
DR RefSeq; WP_012843953.1; NC_013501.1.
DR AlphaFoldDB; D0MIN4; -.
DR SMR; D0MIN4; -.
DR STRING; 518766.Rmar_1455; -.
DR PRIDE; D0MIN4; -.
DR EnsemblBacteria; ACY48342; ACY48342; Rmar_1455.
DR KEGG; rmr:Rmar_1455; -.
DR eggNOG; COG0342; Bacteria.
DR HOGENOM; CLU_007894_4_3_10; -.
DR OMA; SEGARIW; -.
DR OrthoDB; 121331at2; -.
DR Proteomes; UP000002221; Chromosome.
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; IPR005791; SecD.
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; PF02355; SecD_SecF; 1.
DR TIGRFAMs; TIGR00916; 2A0604s01; 1.
DR TIGRFAMs; TIGR01129; secD; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..622
FT /note="Protein translocase subunit SecD"
FT /id="PRO_5000530340"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 559..579
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 584..604
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
SQ SEQUENCE 622 AA; 68193 MW; 61090BAC75EC8F5D CRC64;
MKRNGFKIGV TLALLLLCGY YLYPTVRYAL LQRKLNRMSE EERAAFIEAN YGTIQSLRER
ALKLGLDLQG GMHVTLEVRV DALIRELATD VDETFEEVLA AARERARSGD VSLIDAFVEE
FERRDPNARL SRYFRNPDAG ITRRSSNEEV AAYLRQQAEE AVNRAIEIIR DRVDRYGVTE
PVIQKQGTRR IVVELPGVDD PERVRRLLRG TARLEFRLMA DPQLLQAALQ DIIAYYEPDT
TAASETSAVT DTATADTSLA ALLGEQPSPE RPRNPLLAVM QPVGQGVVFG IVAGPDTAQV
NRLLRNPEVQ ALLPSGIELL YTANPVGTDE QGRPLYYLLG VRKEVELTGE VITDARVEFD
ELNRPQVSMT MNSEGARIWA RLTGANVGKH IAIVLDNVVY SYPVVNERIP SGRSSITGLD
SREEAQDIVT VLKSGALPAP VDIIEERTVG PSLGEASIRA GLRSVLTGLL LVALFMIFYY
RTGGMIADLA LVLNIIFILG ILAAFNATLT LPGIAGIVLT IGMAVDANVL IFERIREEQA
TGKTLRAAID LGYSKAFSAI FDANITTFFT AAILYSFGVG PIQGFAVTLM AGIAASLFSA
IVITRIIFDY LVLERKLMVS VG