ID A0A1I3PTA1_9RHOB Unreviewed; 875 AA.
AC A0A1I3PTA1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=SAMN04488138_10371 {ECO:0000313|EMBL:SFJ25024.1};
OS Celeribacter halophilus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=576117 {ECO:0000313|EMBL:SFJ25024.1, ECO:0000313|Proteomes:UP000183299};
RN [1] {ECO:0000313|EMBL:SFJ25024.1, ECO:0000313|Proteomes:UP000183299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.8891 {ECO:0000313|EMBL:SFJ25024.1,
RC ECO:0000313|Proteomes:UP000183299};
RA de Groot N.N.;
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; FORY01000003; SFJ25024.1; -; Genomic_DNA.
DR RefSeq; WP_066607516.1; NZ_QKZJ01000003.1.
DR AlphaFoldDB; A0A1I3PTA1; -.
DR STRING; 576117.SAMN04488138_10371; -.
DR OrthoDB; 9805019at2; -.
DR Proteomes; UP000183299; 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:UP000183299};
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 445..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 696..716
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 723..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; 93996 MW; 0169B94561ECAD33 CRC64;
MLQMPLWKRI VIWGLVALGL LAALPNAFYP RVEGHNDAIA AIEKAGETPE RAAARDAWPS
FLPSSLVNLG LDLRGGAHLL GEVDVAEVYA SRMDAYWPEV RDALRDERDT VGTIRRLDAP
DGQLRVRISN PEGMETALAA VRALGTSVVS LTSAGEKDID VSATGDVITV QLSEAEKAAT
DDRTMQQSLE IIRRRVDEVG TREPTIQRQG ENRILIQVPG IGSAAELKSL IGTTAQLTFN
PVVGRTTNPD ENPGARNFIA PSINEPGIYY ILEQSAVVTG DELTDSQPAF DQNGRPSVTF
RFNPTGARKF GEYTAANVGA LFAIVLDDEV ISAPRIQDAI RGGSGQITGS FTVEESTELA
VLLRAGALPA KINFLEERTI GPELGADSIE AGRIATTVAF VAVLVFMGAA YSLFGMFANI
ALIINVALLF GLLSAIGATL TLPGIAGIVL TVGMAVDANV LIFERIREEL KNSKSVGRAI
ELGYEKALSA IIDANITTFI TAAILFVMGS GPVKGFAVTL ALGLITSVFT AIYVTRAMVV
AWYGRKNRKG WMLKGVSLVP SETTFDFFKT QKFTFGFSGA LVVAAVVAFF AMGLNFGIDF
KGGTTIRTQS ESAVDVGDYR VALEGLELGD VSITEVFDPN FEENQHVAMV RIQAQDDVEA
ITPETVQLVE KALQEVDPSI TFPSVESVGP KVSGELIWTA VEAVAAAIAA VLFYIWLRFE
WQFAVGAVVA LVHDVAITIG IFALFGIQFD LTIIAALLTI VGYSLNDTVV VFDRVRENLR
RYKKLDLAQV LNMSINETLS RTVMTSGTTL IALIALLVLG GDVIRGFVFA MTLGVVVGTW
SSVFVASTVL LWFGVKRDWD KKEPAKGIQT DGSAV
//
