ID A0A521BJG2_9BACT Unreviewed; 607 AA.
AC A0A521BJG2;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN ORFNames=SAMN06265219_102335 {ECO:0000313|EMBL:SMO47307.1};
OS Gracilimonas mengyeensis.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae; Gracilimonas.
OX NCBI_TaxID=1302730 {ECO:0000313|EMBL:SMO47307.1, ECO:0000313|Proteomes:UP000317557};
RN [1] {ECO:0000313|EMBL:SMO47307.1, ECO:0000313|Proteomes:UP000317557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21985 {ECO:0000313|EMBL:SMO47307.1,
RC ECO:0000313|Proteomes:UP000317557};
RA Varghese N., Submissions S.;
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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. Other proteins may also be involved.
CC {ECO:0000256|HAMAP-Rule:MF_01463}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01463};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01463}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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; FXTP01000002; SMO47307.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A521BJG2; -.
DR OrthoDB; 9805019at2; -.
DR Proteomes; UP000317557; Unassembled WGS sequence.
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; 3.30.70.3220; -; 1.
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; 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; 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 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:UP000317557};
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 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 445..464
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 471..490
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 496..517
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 538..564
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 570..593
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 163..221
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 426..597
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 607 AA; 66183 MW; 1FC14B6FB4A22268 CRC64;
MQGNGFKIGS IVAFLALTIY YLLPTIQWTL EQNYIDDLSP SEAAEYREEN GEDLEELRAN
TLSLGLDLQG GMHVTLEVGV PQLVQELAGE NADQLLTDVI QTARDQSIET GEDFIDLMVA
EFESRDPDAR LSRYYRNDAM DITRRSTNEE IATYLKNQRE SALERAIEII RTRVDRYGVT
EPSIVKQGQS RIVVELPGVE DKERVRNLLK GTARLEFRLA ADANEFSSFV DQLYTYYDTY
QDADADSAQT DSAAQSQFNP LEEVLVPAQS PYLVGYATPE DTARVMDLLR TQDIQRMMPR
NTTVMWSANP LPGQSGQDLY QLIGVRTQIE LTGEVIEAAS VQFDPATNVP EVSMSMNSEG
ARKWGRITGA NIGKPVAIVL DGYVFSYPNV QTKISNGRSS ITGLDGVQEA EDLVNILLSG
ALPAPLEILE ERTVGATLGA ESISAGLNSV LVGLGIVAIF MIVYYRTGGG IADLALLLNI
IFILGILAAF KATLTLPGIA GIVLTIGMAV DANVLIFDRI REEQRTGKTM KASIEAGYSN
AMSAIIDANV TTFFVAIILF SFGVGPIKGF AVTLMAGIVA SLFSAIVITR VIVDYLSQNK
PSTVTFG
//