ID K0P5X1_9BACT Unreviewed; 967 AA.
AC K0P5X1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
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 ECO:0000313|EMBL:CCM10218.1};
GN Synonyms=secF {ECO:0000256|HAMAP-Rule:MF_01464};
GN ORFNames=CAHE_0441 {ECO:0000313|EMBL:CCM10218.1};
OS Cardinium endosymbiont cEper1 of Encarsia pergandiella.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Amoebophilaceae;
OC Cardinium.
OX NCBI_TaxID=1231626 {ECO:0000313|EMBL:CCM10218.1, ECO:0000313|Proteomes:UP000003996};
RN [1] {ECO:0000313|EMBL:CCM10218.1, ECO:0000313|Proteomes:UP000003996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zchori-Fein et al. 2004 {ECO:0000313|Proteomes:UP000003996};
RX PubMed=23133394; DOI=10.1371/journal.pgen.1003012;
RA Penz T., Schmitz-Esser S., Kelly S.E., Cass B.N., Muller A., Woyke T.,
RA Malfatti S.A., Hunter M.S., Horn M.;
RT "Comparative Genomics Suggests an Independent Origin of Cytoplasmic
RT Incompatibility in Cardinium hertigii.";
RL PLoS Genet. 8:e1003012-e1003012(2012).
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. Other proteins may also be involved.
CC {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. 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 -!- 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; HE983995; CCM10218.1; -; Genomic_DNA.
DR AlphaFoldDB; K0P5X1; -.
DR STRING; 1231626.CAHE_0441; -.
DR KEGG; che:CAHE_0441; -.
DR PATRIC; fig|1231626.3.peg.439; -.
DR eggNOG; COG0341; Bacteria.
DR eggNOG; COG0342; Bacteria.
DR HOGENOM; CLU_007894_3_0_10; -.
DR Proteomes; UP000003996; 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 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 InterPro; IPR000731; SSD.
DR NCBIfam; TIGR00916; 2A0604s01; 1.
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.
DR PROSITE; PS50156; SSD; 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};
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 14..35
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 483..502
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 507..527
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 533..554
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 582..600
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 606..630
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 667..685
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 798..816
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 823..845
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 857..877
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 908..928
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 934..956
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 827..957
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
SQ SEQUENCE 967 AA; 107325 MW; 34F9EF51CD9A044A CRC64;
MHSSILASMK SKKIVFFLAI VTTLLSLYYL SFTFIDYRVQ RQAEKQAMDE QGRVDFDKSQ
AYLMKIWKKP VCNLLGTVYT YEEVKERSLK LGLDLQGGMQ VTMEVMPVEL VKRLAAYPTD
PLFLEALQCA QHQREKGTTT SFGKLFVAAY KKLAPNGNLK DIFATAQVGP YIFSSEDDII
KAIDQIISKA LDRSLAIVGA RLDRFGATQT TMQKLPGSER IQIELPGVTH PERVKKLLQG
VAQLRFWTVE EANEYGPLLE AVNNFLLDKE KETILLTFPK ALTEEEKNQR LPKASIIKRI
CKDTFPYRLA YAPEEMDQID AILHSKPVKA LLPKNITWMW DKKAITLGDG TKAVVLYAIQ
LSRENQPLLE GDIITDATQS FAENGKPFVM IQMNQKGARI WKRITASHIG KRIAITLDDR
VYTAPVVNQE IPNGVSKIIG DFTLEEAKDL ASVLQTGALP APLKVVEEAI MGPSLSKVAQ
NQGLMATAVG LGLVLLFMLI YYAKGGIIAN VALLLNLLFM VAILAQLEAT LTLPGIAGLV
LTIGMSIDAN VLIFERIREE LEQKVSIKEA IQHGYTKSYG SIIDANITTF LAGAILYYLG
QGPVRGFALI LMLGIITSIF TSIFITRLIF SFFIDTYSIP NLTFSYPTIP RLFKNVQIDF
IKNRYRFYLC SLLFIAIGGC CFYHYKGLTL GVDFAGGRSY TVHFCKPIDA SLLKEGLSYR
YKESVEVRTY GANNVMQITT SYLRDEDASD KKVLNKLVAA LKDLTQLEEN NNLSTGNDFR
ITSSTRVGAT VAHDVQKSAQ KAILLAILGI FFYIRIRFRR PGFGLAAVVA LVHDVLAVIA
GFCIARGFGL NYEVNEVFLA AMLTVIGYSI NDTVVIYDRI REKLANKAMG MSPHIINDAI
RETLSRTVIT SFTTLLAIAV LFFFGGAALQ GFSFALTLGV LFGTYSSICI AAPLLADFGR
KLSATKQ
//
