ID A0A167ULX2_9FLAO Unreviewed; 990 AA.
AC A0A167ULX2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=FBFR_14425 {ECO:0000313|EMBL:OAB25695.1};
OS Flavobacterium fryxellicola.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=249352 {ECO:0000313|EMBL:OAB25695.1, ECO:0000313|Proteomes:UP000077164};
RN [1] {ECO:0000313|EMBL:OAB25695.1, ECO:0000313|Proteomes:UP000077164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16209 {ECO:0000313|EMBL:OAB25695.1,
RC ECO:0000313|Proteomes:UP000077164};
RA Shin S.-K., Yi H.;
RT "Draft genome sequence of Flavobacterium fryxellicola DSM 16209.";
RL Submitted (MAR-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. 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}.
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:OAB25695.1}.
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DR EMBL; LVJE01000044; OAB25695.1; -; Genomic_DNA.
DR RefSeq; WP_066082562.1; NZ_LVJE01000044.1.
DR AlphaFoldDB; A0A167ULX2; -.
DR STRING; 249352.SAMN05444395_10894; -.
DR OrthoDB; 9805019at2; -.
DR Proteomes; UP000077164; 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; 3.30.70.3220; -; 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:SF1; PROTEIN TRANSLOCASE SUBUNIT SECD; 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};
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 493..510
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 517..540
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 546..564
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 585..611
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 623..642
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 676..694
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 814..831
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 838..859
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 874..893
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 924..942
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 948..972
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 184..240
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 473..642
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
FT DOMAIN 792..974
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 990 AA; 108069 MW; 898B3604B54F9275 CRC64;
MQNKGLIKFF AILFALVSIY QLSFTFVASK VKNDAKSFAN GNADKEVKYL DSIGKEKVFN
LGFTNFTFNE VSDKQINKGL DLEGGINVIL QISVKDILKG LSNNSKNPVF NKSLADATAD
LQGNKSYLDK FFDAFEANSK GTVKLASPDI FANRSLQGEG GVDFQMTDSE VQKVIKRKVD
ESVESAFGVL RKRIDQFGVT QPNIQKLGNS GQILVELPGA KDVDRAKKLL SSTAQLQFWE
TYKIEEIGNF LMAANESLKK TEINITEVKP VVKDSLSALL TDSKDSTAAK KGGNPLFDKI
VGQGGGPVLG LFSPKDTATI NGYLKRADIR ILLPAEQRYA KFVWGIPTTI KDAKAKDVEV
LELYALKGNR DNVPAMAGGV ITDAKDTFDQ SGKPAVSMQM NGQGAKSWEE LTGRAYTQKS
NIAIVLDDVV YSAPGVSSGP ISGGRSEISG AFDVTQTKDL ANVLRAGKLP ATADIVQSEV
VGPSLGQEAI DNGTNSAIIG LLIVSLWMMI YYGKAGWYAN IALAINLLFL FGILASLGAV
LTLPGIAGIV LTMGTAVDAN IIIYERAKEE LRAGKTLEEA VKTSYSWRGA MSSITDANVT
HILTGAVLFI FGSGPIKGFA TTLLIGIITS LFTSIFIARI FIDWNISKKN NLTFVTNFSK
NMFNNFHFDF LGMKKWTYLF SSIVVIISVV SLATNGLDQG VDFVGGRTFQ VRFEKPIETE
TVKAELAQVF EGSAEVKVFG NTNQLKITTK YKVQEPGIKA DEEVNKLLFS TLKKHYSADI
TYDKFVNAYE GKKVGILQAS KVGPTVAEDI KTNAYWAVLG AMAIVFLYLM ISYRKWQYSL
GAIAAVAHDV IFVLGIYSLC YKFMPFGMEI DQHFIAAILT VIGYSMNDTV IVFDRVREYL
AGKTKGTFAE IVNQSINTTM SRTINTSLTM IVVLLIMFVF GGESIRGFIF AMLVGIIVGT
YSSLFIATPV LVDTISKEDK RKVEKAHQES
//
