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Database: UniProt
Entry: M7MRK1_9MICC
LinkDB: M7MRK1_9MICC
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ID   M7MRK1_9MICC            Unreviewed;       577 AA.
AC   M7MRK1;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Name=secDF {ECO:0000313|EMBL:EMQ97651.1};
GN   Synonyms=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   ORFNames=ADIAG_03031 {ECO:0000313|EMBL:EMQ97651.1};
OS   Paeniglutamicibacter gangotriensis Lz1y.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Paeniglutamicibacter.
OX   NCBI_TaxID=1276920 {ECO:0000313|EMBL:EMQ97651.1, ECO:0000313|Proteomes:UP000012015};
RN   [1] {ECO:0000313|EMBL:EMQ97651.1, ECO:0000313|Proteomes:UP000012015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lz1y {ECO:0000313|EMBL:EMQ97651.1,
RC   ECO:0000313|Proteomes:UP000012015};
RX   PubMed=23766407;
RA   Shivaji S., Ara S., Bandi S., Singh A., Kumar Pinnaka A.;
RT   "Draft Genome Sequence of Arthrobacter gangotriensis Strain Lz1yT, Isolated
RT   from a Penguin Rookery Soil Sample Collected in Antarctica, near the Indian
RT   Station Dakshin Gangotri.";
RL   Genome Announc. 1:e00347-e00313(2013).
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:EMQ97651.1}.
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DR   EMBL; AOCK01000009; EMQ97651.1; -; Genomic_DNA.
DR   RefSeq; WP_007272198.1; NZ_AOCK01000009.1.
DR   AlphaFoldDB; M7MRK1; -.
DR   STRING; 1276920.ADIAG_03031; -.
DR   PATRIC; fig|1276920.7.peg.3034; -.
DR   eggNOG; COG0342; Bacteria.
DR   Proteomes; UP000012015; 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:UP000012015};
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        333..353
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        360..382
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        388..411
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        440..457
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        463..482
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          315..492
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
FT   REGION          527..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..553
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..577
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   577 AA;  61419 MW;  9A6AE84E0013899B CRC64;
     MSSTGPIKQA RKSLLWLGVI FLISAAILIT GVLSGKAALA PKLALDLEGG TQMILAPRVA
     GGDAATQEQL DQAVEIIRQR VDGTGVSEAE ITTQSGRNVV VSMPGIPDTR TRELIQASAN
     MEFRAVILAG SFTAVPEDQR LAKADLPKPT AKPENGSDVN WVDAALYQKF EKFDCPTELG
     QRSDEEHEAD EPMISCDPDV GQKYILGPVE VPGADISDSS FSMARGQQGA VTGQWAVNLE
     FNADGTKKFA EVTQRLTALE GAQNQFAIVL DGTVISAPRS NAVIPDGKAQ ITGNFTEESS
     KALADQLKFG ALPISFEIQS EQQISATLGS DQLRSGLIAG IIGLILVAIY SIFQYRLLGV
     VTIVSLLVSG VLTYLALVLL GWSMNYRLSL AGVAGLIVAI GLIADSFIVY FERIRDELRD
     GRPLPSAVEI GWKRAKRTIL ASKAVNILAA VVLYIVAVGN VRGFAFTLGL TAVVDIIVVF
     LLTHPILQLL GKTKFFGEGH RFSGLDPSLL GVVPLYRGAG KVRSFSPEAE GARGKKNAKA
     ASEATRRQTI AERRKAATSV SAPTTQDDSA DKDSTNG
//
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