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Database: UniProt
Entry: A0A081N0Y9_9GAMM
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ID   A0A081N0Y9_9GAMM        Unreviewed;       620 AA.
AC   A0A081N0Y9;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
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:KEQ12112.1};
GN   ORFNames=GZ78_28150 {ECO:0000313|EMBL:KEQ12112.1};
OS   Endozoicomonas numazuensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Endozoicomonadaceae; Endozoicomonas.
OX   NCBI_TaxID=1137799 {ECO:0000313|EMBL:KEQ12112.1, ECO:0000313|Proteomes:UP000028073};
RN   [1] {ECO:0000313|EMBL:KEQ12112.1, ECO:0000313|Proteomes:UP000028073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25634 {ECO:0000313|EMBL:KEQ12112.1,
RC   ECO:0000313|Proteomes:UP000028073};
RA   Neave M.J., Apprill A., Voolstra C.R.;
RT   "Whole Genome Sequences of Three Symbiotic Endozoicomonas Bacteria.";
RL   Submitted (JUN-2014) 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-YajC and YidC. {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:KEQ12112.1}.
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DR   EMBL; JOKH01000011; KEQ12112.1; -; Genomic_DNA.
DR   RefSeq; WP_034842996.1; NZ_JOKH01000011.1.
DR   AlphaFoldDB; A0A081N0Y9; -.
DR   STRING; 1137799.GZ78_28150; -.
DR   eggNOG; COG0342; Bacteria.
DR   OrthoDB; 9805019at2; -.
DR   Proteomes; UP000028073; 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; 3.30.70.260; -; 1.
DR   Gene3D; 3.30.70.3400; -; 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; IPR027398; SecD-TM.
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; PF13721; SecD-TM1; 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:UP000028073};
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        463..480
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        487..505
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        511..532
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        553..574
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        586..609
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   DOMAIN          2..104
FT                   /note="SecD export protein N-terminal TM"
FT                   /evidence="ECO:0000259|Pfam:PF13721"
FT   DOMAIN          231..288
FT                   /note="Protein translocase subunit SecDF P1"
FT                   /evidence="ECO:0000259|Pfam:PF21760"
FT   DOMAIN          441..606
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
FT   REGION          325..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   620 AA;  68178 MW;  B7286406B8B17B4B CRC64;
     MLNRYPLWKY LLIAMIVALG FVYALPNLYP DDPAIQISGA SSSETITAGV QAKAQKALDA
     ANIEAKASDT ENNALLIRLK HADQQQLAKS VIKDALGDDY IVAINLAPTT PDWLTSIGAY
     PMKLGLDLSG GVHFQLEVDT DRAVKTKLDI SNTEIRALLR KERLRYRTMP DRTDGARQLA
     FLDEATRDKA ERRIKREFPD LLVETEDLGE RYVVSYRYSE QYIRELEDYA VKQNLTTVRN
     RVNELGVSEP LVQRQGRNNI VVELPGVQDT AEAKRILGKT ANLEFRLEAL ANASRSNTES
     FDYRGRSVNL ERDIIITGER VSSAQSNFDT ESGQPQVNIS LDSTGGKKMN NATRNNIGRS
     MAVIFIEQKP VTRTETREVD GEKVKVKVPG FREERRVISL ATVQSALGNQ FRITGLDSSG
     EASELALLLR AGSLAAPMYF VEERTVGPSL GAENIKMGVD STLMGLGMVV MFMMVVYRVF
     GLLANIALAI NLMLLTAAMS IFGATLTMPG IAGIVLTLGM AVDANVLVFS RIREEIKLGR
     PVQRAIHDGY DRAFVSIFDG NITTLLVGLI LFAVGTGPIK GFAVTLSIGI VTSMFTAIMV
     TRSLVNLVYG GRRDLKKLSI
//
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