ID A0A1Q5PNZ9_9ACTO Unreviewed; 612 AA.
AC A0A1Q5PNZ9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN ORFNames=BSR29_04755 {ECO:0000313|EMBL:OKL49145.1};
OS Boudabousia liubingyangii.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Boudabousia.
OX NCBI_TaxID=1921764 {ECO:0000313|EMBL:OKL49145.1, ECO:0000313|Proteomes:UP000186785};
RN [1] {ECO:0000313|EMBL:OKL49145.1, ECO:0000313|Proteomes:UP000186785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VUL4_2 {ECO:0000313|EMBL:OKL49145.1,
RC ECO:0000313|Proteomes:UP000186785};
RA Meng X.;
RT "Actinomyces gypaetusis sp. nov. isolated from the vulture Gypaetus
RT barbatus in Qinghai Tibet Plateau China.";
RL Submitted (NOV-2016) 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: 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:OKL49145.1}.
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DR EMBL; MQSV01000002; OKL49145.1; -; Genomic_DNA.
DR RefSeq; WP_073709133.1; NZ_MQSV01000002.1.
DR AlphaFoldDB; A0A1Q5PNZ9; -.
DR STRING; 1921764.BSR28_04320; -.
DR Proteomes; UP000186785; 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; 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 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:UP000186785};
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..33
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 396..413
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 420..442
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 448..471
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 504..526
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 532..551
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 76..132
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 376..550
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
FT REGION 194..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 612 AA; 65928 MW; 38872F37F7B0E6EE CRC64;
MADTRIKKAR RPLIVFLTIL VIAAITLGVG SYLGKASWKP KLALDLEGGT QLVLTPTATE
GKVAKDGRTE VTNEDLNQAI DIIRQRVDAS GVSEAEITSQ GGQNIVVSLP GKPSEETLNL
VRKSAVMVFR SVLRDSHQVA AVSPKAFEEQ AKQLAVTPEG PQKPEETAQR LAALKQAEEL
SKLTPEEIAT RLADENHDGK ISDAPVSAPK DNSDPAWITE KTLYDFYLLD CSDPTKLNDN
RIEPDDKAIA ACGSEGHSKY ILSPVDIQGS EIKNATAGLE HSGPNGATTG QWEVVLEFNS
KGTDQFTQVS QRLFNLKATD PVRSRFAIML DGVVISAPSM NAVISGGSAQ ITGNFNSKSA
TALANQLKFG SLPLTFKVES EQQISATLGS DHLQKGLWAG LIGLLLVIVY LAWSYHGLAL
VALGSLLMAA ISTYLAVVLL GWQMGYRLSL PGVTGLIISI GITADSFIVY FERIRDEVRD
GANLVNAVET GWEHAKKTIL ISDAVNILAA VILYVLAVGG VQGFAFTLGL TTLIDLAVIF
MFTHPILVML LKVPFFGEGR KWSGFDAETL GATPTIYAGR GRVRAPHERR SIADRRAERK
NEAESANEEE AN
//
