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Database: UniProt
Entry: A0A387C333_9MICO
LinkDB: A0A387C333_9MICO
Original site: A0A387C333_9MICO 
ID   A0A387C333_9MICO        Unreviewed;       581 AA.
AC   A0A387C333;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-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:AYG04961.1};
GN   ORFNames=D7I44_16475 {ECO:0000313|EMBL:AYG04961.1};
OS   Gryllotalpicola protaetiae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Gryllotalpicola.
OX   NCBI_TaxID=2419771 {ECO:0000313|EMBL:AYG04961.1, ECO:0000313|Proteomes:UP000275069};
RN   [1] {ECO:0000313|EMBL:AYG04961.1, ECO:0000313|Proteomes:UP000275069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2DFW10M-5 {ECO:0000313|EMBL:AYG04961.1,
RC   ECO:0000313|Proteomes:UP000275069};
RA   Heo J., Kim S.-J., Kwon S.-W.;
RT   "Genome sequencing of strain 2DFW10M-5.";
RL   Submitted (SEP-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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01463}.
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DR   EMBL; CP032624; AYG04961.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A387C333; -.
DR   KEGG; gry:D7I44_16475; -.
DR   OrthoDB; 5240379at2; -.
DR   Proteomes; UP000275069; 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   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:UP000275069};
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        350..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        377..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        405..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        457..474
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        480..499
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   DOMAIN          70..126
FT                   /note="Protein translocase subunit SecDF P1"
FT                   /evidence="ECO:0000259|Pfam:PF21760"
FT   DOMAIN          332..507
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
FT   REGION          131..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   581 AA;  61074 MW;  F4DA12EC73F23FC6 CRC64;
     MAKTSPVRHA SRSLIWLGVL VVALAAALTS GVLWGSATVA PKLGLDLQGG TEVILTPALA
     GNQQITSDEL DQAVSIIRQR VNASGVSEAT VSTQGNTNIV VDVPGRLDDA TKQRIEASSK
     MELRPVLLAE SPATTSFTGQ DGKQTPYPTP APTLANTPTA KPTDASDPSW VTPYLQAKYD
     AFDCATLKDA TTNVAPAGEP LVTCDDAGQT KYLLGPVEVQ GSDITNATAG MISSQQGVTT
     GQWGVNLTFN STGAKAFDKV SQRLNGYYVA AQSAGTNDPR SQFAFVLDGR VLEAPQMQGI
     ITGNTSQITG SFTQASAQTL ANQLKFGALP VSFKVQSSNT ISATLGSAQL LSGVIAGAIG
     LLLVFIYTLF QYRTLGFVTI ASLVIAAALS YLTISLLSWQ MGYRLSLAGV AGLIVAIGFT
     ADSFIVYFER IRDELREGRG LESAVEAGWK RARRTVYAAK TTNLLAAVVL YIFAVGDVQG
     FAFTLGLTTI LDVIIVVLFT HPIMQLFART EFFASGHKLS GLDPTALGAV YRGAGQFRPS
     TAVGAGKLAS SSREAAKRQT IAERKAAELA AAGTRRNGKD D
//
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