ID K9D146_9FIRM Unreviewed; 418 AA.
AC K9D146;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN ORFNames=HMPREF9282_01581 {ECO:0000313|EMBL:EKU78023.1};
OS Veillonella seminalis ACS-216-V-Col6b.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=883156 {ECO:0000313|EMBL:EKU78023.1, ECO:0000313|Proteomes:UP000009891};
RN [1] {ECO:0000313|EMBL:EKU78023.1, ECO:0000313|Proteomes:UP000009891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-216-V-Col6b {ECO:0000313|EMBL:EKU78023.1,
RC ECO:0000313|Proteomes:UP000009891};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Veillonella ratti ACS-216-V-COL6B.";
RL Submitted (SEP-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:EKU78023.1}.
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DR EMBL; AHAF01000016; EKU78023.1; -; Genomic_DNA.
DR RefSeq; WP_006556468.1; NZ_JH992937.1.
DR AlphaFoldDB; K9D146; -.
DR STRING; 883156.HMPREF9282_01581; -.
DR GeneID; 83055195; -.
DR PATRIC; fig|883156.3.peg.1540; -.
DR eggNOG; COG0342; Bacteria.
DR HOGENOM; CLU_007894_4_2_9; -.
DR OrthoDB; 9805019at2; -.
DR Proteomes; UP000009891; 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; 3.30.70.3220; -; 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};
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 238..256
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 287..311
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 332..354
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 360..384
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 60..118
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 216..388
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 418 AA; 45152 MW; C6AE72B07561C50E CRC64;
MNGKALAKFL AVIALIFAAF IYFIGPLAQS IKQGLDLQGG THIVLEAEDA GENKVTDDAV
ERARQILERR INEMGLAEPL IQREGKKRII IELPGVKDPD QAIKTIGKTA VMEFKDENGV
VHLTGNDLKD AKEQIGQNKQ FMVAIEFTDE GAKKFADLTT QNVGRHIGIY LDGEQLTNPV
VNEPITGGKA VITGSKTLDE AKNLAILLRS GALPVKVNVL EVRTVGPTLG QDSKDKSVTA
FAVGIGLIVA FMLVLYRVSG FVATTALLIY VLLLLAVLHF LQATLTLPGI AGIILSMGVA
VDANILIFER FKEEVQIGKT LRMSMESGFR RALATIVDAN MSVMITAAIL FILGSGPVRG
FAITLGLGVA ISMVTAVFVS RYLLRMLIEC NLTNHPFWYG ANVSPTATME LYKKGGKK
//
