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Database: UniProt
Entry: W0EVZ2_9BACT
LinkDB: W0EVZ2_9BACT
Original site: W0EVZ2_9BACT 
ID   W0EVZ2_9BACT            Unreviewed;      1047 AA.
AC   W0EVZ2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
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=NIASO_06985 {ECO:0000313|EMBL:AHF14972.1};
OS   Niabella soli DSM 19437.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Niabella.
OX   NCBI_TaxID=929713 {ECO:0000313|EMBL:AHF14972.1, ECO:0000313|Proteomes:UP000003586};
RN   [1] {ECO:0000313|EMBL:AHF14972.1, ECO:0000313|Proteomes:UP000003586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19437 {ECO:0000313|Proteomes:UP000003586};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (DEC-2013) 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. 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; CP007035; AHF14972.1; -; Genomic_DNA.
DR   RefSeq; WP_008585070.1; NZ_CP007035.1.
DR   AlphaFoldDB; W0EVZ2; -.
DR   STRING; 929713.NIASO_06985; -.
DR   KEGG; nso:NIASO_06985; -.
DR   eggNOG; COG0341; Bacteria.
DR   eggNOG; COG0342; Bacteria.
DR   HOGENOM; CLU_007894_3_0_10; -.
DR   OrthoDB; 9805019at2; -.
DR   Proteomes; UP000003586; 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   NCBIfam; TIGR00916; 2A0604s01; 2.
DR   NCBIfam; TIGR01129; secD; 1.
DR   NCBIfam; TIGR00966; transloc_SecF; 1.
DR   PANTHER; PTHR30081:SF8; PROTEIN TRANSLOCASE SUBUNIT SECF; 1.
DR   PANTHER; PTHR30081; PROTEIN-EXPORT MEMBRANE PROTEIN SEC; 1.
DR   Pfam; PF07549; Sec_GG; 1.
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:UP000003586};
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        7..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        552..571
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        576..598
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        604..626
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        647..669
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        681..699
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        733..753
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        865..883
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        890..912
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        924..945
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        976..994
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        1000..1024
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   DOMAIN          210..266
FT                   /note="Protein translocase subunit SecDF P1"
FT                   /evidence="ECO:0000259|Pfam:PF21760"
FT   DOMAIN          532..701
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
FT   DOMAIN          844..1027
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
SQ   SEQUENCE   1047 AA;  115842 MW;  6EE766AF20BABD5B CRC64;
     MQLKGLVRFF TILLIIYSLY QLSFTWFVRN HEKKLETIAN RYVNTNYATA AQKYPSNKDS
     QEVYQEKLNH IYNDRLTRLK DSTKDETITY GITGAISYQK AKEEELNLGL DLQGGMNVTL
     EVEMSGLLKT LANNSNDPNF LKALENADKR RANSNANFIN LFVEEFKKLS PSTPLAAVFA
     TANHESIKVT DSDDKVVRFL QEQARAAFDN TAKLITTRID KFGVAQPSIN PDPVKQIINV
     ELPGVQDKER VRKNLQASAN LQFWEVYNIS ELWPNLQKAD ELFFAQNSGK AATDSTAKTD
     SAATQHAGAD SAKALASDTS KKLEDQLKQL ATADKNANKP AAATTNQEAE AKKHLWGWLL
     PAMDQQGRLA DMGLIGQVNI KDTAAVREIL ESAALKAQFP SEVAWMYGIP ERVGTGNKKS
     NMVALYAIKT YGKDKAKLEG EHVTNAGYDF DQTGKTNVSL EMDALGSRIW ADMTRANIKK
     HIAIVVDNQV YSAPVVNDAI EGGRSSISGN FTQEEAKDLA NILKIGKLPA PAKIVSDETV
     GPTLGQAAIK GGLMSFTLSF IVIFILMLIY YNTSGWIANI ALILNLLFTV GVLAGLGATL
     TAPGIAGLVL TIGMAVDSNV IIYERIKEEL TKGKGYITAI NEGYSRSLAP VLDGHVTTLI
     TAFILYYFGL GPVKGFATTQ ILGLLLSLFC GILVSRWVTD WFTNKNHHLK YFTSLSRSIF
     KHSAFKFIEF RKVAYAISVV ILLLSVGTIF HGFDYGVEFD GGRSYRVDFG KKVNVEQLRD
     DLKKTFDNEN PSIKTVGDES ALDITTSYLI KDPNSQRADS IVVQKLYNGL KAYLPAGTSF
     AQFDNQYKLS SKIVLPTISD DLKKGAVRAT ILALIAIFLY IFLRFRDWRY SLGTIFSLLH
     DALVVLIVFS YFRDHVPFPL EIDQHFIAAI LTVIGFSMND TVVVFDRIRE DGRLYPGLDQ
     KQLVNKAIND TLSRTIMTSL TVFITVLILF IFGGEAVRGF AFAMLIGVVT GVYSSIFVAA
     PVLVDLKGGL KRNKHKAVTA KVRPEHN
//
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