ID K6VF77_9MICO Unreviewed; 633 AA.
AC K6VF77;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000256|HAMAP-Rule:MF_01463,
GN ECO:0000313|EMBL:GAB94813.1};
GN ORFNames=KILIM_011_00860 {ECO:0000313|EMBL:GAB94813.1};
OS Kineosphaera limosa NBRC 100340.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC Kineosphaera.
OX NCBI_TaxID=1184609 {ECO:0000313|EMBL:GAB94813.1, ECO:0000313|Proteomes:UP000008366};
RN [1] {ECO:0000313|EMBL:GAB94813.1, ECO:0000313|Proteomes:UP000008366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100340 {ECO:0000313|EMBL:GAB94813.1,
RC ECO:0000313|Proteomes:UP000008366};
RA Yoshida I., Isaki S., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y.,
RA Ohji S., Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Kineosphaera limosa NBRC 100340.";
RL Submitted (AUG-2012) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01463}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAB94813.1}.
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DR EMBL; BAHD01000011; GAB94813.1; -; Genomic_DNA.
DR RefSeq; WP_006591345.1; NZ_BAHD01000011.1.
DR AlphaFoldDB; K6VF77; -.
DR STRING; 1184609.KILIM_011_00860; -.
DR eggNOG; COG0342; Bacteria.
DR Proteomes; UP000008366; 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 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 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; PF21760; SecD_1st; 1.
DR Pfam; PF02355; SecD_SecF; 1.
DR PRINTS; PR00702; ACRIFLAVINRP.
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:UP000008366};
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 430..450
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 457..479
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 485..508
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 536..554
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 560..584
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 68..123
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 412..587
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
FT REGION 131..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 633 AA; 66373 MW; 3228C6DDA6DBD88E CRC64;
MANPKTRPFR STLAIFTLIT LMLTGGLIAS VQFSDGSWTP KLGLDLEGGT QMVLQPQTAD
GTVNAEQLDQ AVDIMRARVD GQGVAEAEVA TLGNNVVVAV PGAMTREQED ALRQSSQMRF
RPVITVVAGS PMEVSPIPGE GDPTEPAADP TAPTPDATEP AASPTGGATA SPATPAPSPT
TAGAVLPRGL QQATPTPTGT PTASPTATPT GSPAATPEPT ETPGLGLPTS EEGTPTITPQ
DAADPQKLIE YASSEAWLTA QWSQRLEEFD CRAQPVYDPS KEDPLQPSVA CSDDGAAKYL
LGPAVISGDQ LADASSGPIV SQQTGAPTGG YQVNLQMDGG EATAAYATVS RYMVGLPEPR
NQLAIVLDNH VVSAPRFENA IPDGRAQITG NFTAESAMAL ANQLKFGALP MSFTVQSTES
VSPTIGGDQL RLAMIAGAVG LLLVVLYSLW QYRALGLVTV ASLLVTAGLT YLVLTLFGWG
YNLRLTMAGI TGAIVAIGTT VDSFIVYFER VRDELRDGRR LQSAVQSGWA RASRTIYISS
AVSFLAATVL YALATSNVRG FAFVLMLTTV LDLFVTVMFT HPLLSLLSHV KFFRDGHRLS
GFHPDTIGAI PAYRGRGRTR LSDSATTPQE VSA
//