ID A0A2R4SYL2_9ACTN Unreviewed; 580 AA.
AC A0A2R4SYL2;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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:AVZ71959.1};
GN ORFNames=SLUN_06865 {ECO:0000313|EMBL:AVZ71959.1};
OS Streptomyces lunaelactis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1535768 {ECO:0000313|EMBL:AVZ71959.1, ECO:0000313|Proteomes:UP000244201};
RN [1] {ECO:0000313|EMBL:AVZ71959.1, ECO:0000313|Proteomes:UP000244201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MM109 {ECO:0000313|EMBL:AVZ71959.1,
RC ECO:0000313|Proteomes:UP000244201};
RA Naome A., Martinet L., Maciejewska M., Anderssen S., Adam D., Tenconi E.,
RA Deflandre B., Arguelles-Arias A., Calusinska M., Copieters W., Karim L.,
RA Hanikenne M., Baurain D., van Wezel G., Smargiasso N., de Pauw E.,
RA Delfosse P., Rigali S.;
RT "Complete genome sequence of Streptomyces lunaelactis MM109T, a Ferroverdin
RT A producer isolated from cave moonmilk deposits.";
RL Submitted (JAN-2018) 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; CP026304; AVZ71959.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R4SYL2; -.
DR KEGG; slk:SLUN_06865; -.
DR OrthoDB; 5240379at2; -.
DR Proteomes; UP000244201; Chromosome.
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 InterPro; IPR000731; SSD.
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.
DR PROSITE; PS50156; SSD; 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:UP000244201};
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 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 434..459
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 487..506
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 512..531
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 406..537
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
FT REGION 137..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 580 AA; 60703 MW; 4248756BDB7C260B CRC64;
MAAPNRGRRP TGAQGKPGRA LVLILIAMVA LTGGMFFAGQ LTPRLGIDLA GGTTITLEAK
NTVANKNAIN ETNMNTAVGI IERRVNGLGV SEAEVQTQGE KNIIVNIPKG TNSQQAREQV
GTTAQLYFRP VLTVAAGTPT APQPTPSASA SGTAKDGKAT ETATPPSGTP TATATTQGRA
VTEALKAPTP TPSGSGAPKS TPTPTPSGDA AAADKLQKDF LALDCRNDKV RGALGDKAKP
SDTTLACGKN SAGEWEKYVL GPAEVSGKDV DDAKGQLDQQ RGMWIVTMDF TNSGSKKFQA
ITSKLSQQQP PMNQFAIVLD GEVVSAPSVN QTLSASAEIS GSFTQESAQD LGNILSYGAL
PLSFEAQSTQ TVSAALGGEQ LQAGLIAGAI GLALVIIYLV AYYRGLALVA ILSLIVSAIL
TYTIMSLLGP GIGFALNLPA VCGAIVAIGI TADSFIVYFE RIRDEIREGR TLRPAVERAW
PRARRTILVS DFVSFLAAAV LFLVTVGKVQ GFAFTLGLTT VLDVVVVFFF TKPIMTLLAR
MKFFADGHPW SGLDPKRLGA KPPLRRSRRA SAPTDHPKEA
//
