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Database: UniProt
Entry: A0A0N9ZD28_9RHOB
LinkDB: A0A0N9ZD28_9RHOB
Original site: A0A0N9ZD28_9RHOB 
ID   A0A0N9ZD28_9RHOB        Unreviewed;       875 AA.
AC   A0A0N9ZD28;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_01463, ECO:0000256|HAMAP-Rule:MF_01464};
DE   Includes:
DE     RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
DE   Includes:
DE     RecName: Full=Protein-export membrane protein SecF {ECO:0000256|HAMAP-Rule:MF_01464};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Synonyms=secF {ECO:0000256|HAMAP-Rule:MF_01464};
GN   ORFNames=IMCC12053_700 {ECO:0000313|EMBL:ALI54648.1},
GN   SAMN05444421_10569 {ECO:0000313|EMBL:SFK52174.1};
OS   Celeribacter marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Celeribacter.
OX   NCBI_TaxID=1397108 {ECO:0000313|EMBL:ALI54648.1, ECO:0000313|Proteomes:UP000064920};
RN   [1] {ECO:0000313|EMBL:ALI54648.1, ECO:0000313|Proteomes:UP000064920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC 12053 {ECO:0000313|EMBL:ALI54648.1,
RC   ECO:0000313|Proteomes:UP000064920};
RA   Wang D.B., Wang M.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SFK52174.1, ECO:0000313|Proteomes:UP000181863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100036 {ECO:0000313|EMBL:SFK52174.1,
RC   ECO:0000313|Proteomes:UP000181863};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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 SecD. 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_01464}.
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   -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01464}.
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; CP012023; ALI54648.1; -; Genomic_DNA.
DR   EMBL; FOSM01000005; SFK52174.1; -; Genomic_DNA.
DR   RefSeq; WP_062215738.1; NZ_FOSM01000005.1.
DR   AlphaFoldDB; A0A0N9ZD28; -.
DR   STRING; 1397108.IMCC12053_700; -.
DR   KEGG; cmar:IMCC12053_700; -.
DR   PATRIC; fig|1397108.4.peg.725; -.
DR   OrthoDB; 9805019at2; -.
DR   Proteomes; UP000064920; Chromosome.
DR   Proteomes; UP000181863; 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; 3.30.70.3400; -; 1.
DR   Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR   HAMAP; MF_01463_B; SecD_B; 1.
DR   HAMAP; MF_01464_B; SecF_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; IPR005665; SecF_bac.
DR   NCBIfam; TIGR00916; 2A0604s01; 2.
DR   NCBIfam; TIGR01129; secD; 1.
DR   NCBIfam; TIGR00966; transloc_SecF; 1.
DR   PANTHER; PTHR30081:SF1; PROTEIN TRANSLOCASE SUBUNIT SECD; 1.
DR   PANTHER; PTHR30081; PROTEIN-EXPORT MEMBRANE PROTEIN SEC; 1.
DR   Pfam; PF07549; Sec_GG; 2.
DR   Pfam; PF21760; SecD_1st; 1.
DR   Pfam; PF02355; SecD_SecF; 2.
DR   PRINTS; PR01755; SECFTRNLCASE.
DR   SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 2.
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:UP000064920};
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        394..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        444..466
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        487..508
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        520..544
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        575..598
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        699..717
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        724..745
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        751..772
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        803..821
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        827..853
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   DOMAIN          185..242
FT                   /note="Protein translocase subunit SecDF P1"
FT                   /evidence="ECO:0000259|Pfam:PF21760"
FT   DOMAIN          371..543
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
FT   DOMAIN          669..854
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
SQ   SEQUENCE   875 AA;  93653 MW;  FCC079FA1A6A2858 CRC64;
     MLQISRWKKI VIWGLVALGL YAALPNAFYA RVEGHNDAVA AIESAGETSE RAAARDAWPS
     YLPTGLVNLG LDLRGGAHLL GEVEVGEVYA ARVDTLWPDV RDALRDERDT VGTIRRLDAP
     DGLLRVRISQ ADGMETALAA VRALASPVVS LTAAGQKDYV VAANNDVITV ELSEAEKAAT
     DTRTMQQSLE IIRRRVDEVG TREPTIQRQG EDRILIQVPG IGSASELKSL IGTTAKLTFN
     PVVGQTSNPD QAPGARNFIA PSLDQAGVYY ILEETPVVSG DELTDSQPAF DQNGRPAVTF
     RFNPTGARKF GDYTAANVGA PFAIVLDNEV ISAPRINEAI RGGSGQITGN FSVEESTELS
     VLLRAGALPA KINFLEERTI GPELGADSIE AGKLATMVAF GAVLIFMGVS YGLFGIFANI
     ALIINVGLLF GLLSMIGATL TLPGIAGIVL TVGMAVDANV LVFERIREEL KTAKGVGRAI
     ELGYEKALSA IIDANITTFI TAAILFIMGS GPVKGFAVTL ALGIMTSVFT AIFVTRAMVV
     MWYGRKNRKG WTLKGLKLVR DDTTVDFFKV AKVTFGFSGA MVVVALVSFL MMGLNFGIDF
     RGGTTIRTQS ESAVDVADYR AALAPLGFGD VSITEVFDPN FAENQHVAMI RIEAQDDVSS
     VAPETIQTVE DALKVVDESI TFPSVESVGP KVSGELIKTA IYAVVAAIAA VLFYIWLRFE
     WQFAVGAVVA LVHDIAITIG IFAIFKIQFD LTIIAALLTI VGYSLNDTVV VFDRVRENLR
     KYKKLELSGV LNMSINETLA RTVMTSGTTL VALIALLVLG GDVIRGFVFA MTLGIVVGTW
     SSVFVASNIL LWLGVKRDWD KKDPTPGIQA DGSAV
//
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