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Database: UniProt
Entry: F0HKL6_9ACTN
LinkDB: F0HKL6_9ACTN
Original site: F0HKL6_9ACTN 
ID   F0HKL6_9ACTN            Unreviewed;      1002 AA.
AC   F0HKL6;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Tat pathway signal sequence domain protein {ECO:0000313|EMBL:EGC90275.1};
GN   ORFNames=HMPREF9404_3142 {ECO:0000313|EMBL:EGC90275.1};
OS   Eggerthella sp. HGA1.
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Eggerthella.
OX   NCBI_TaxID=910311 {ECO:0000313|EMBL:EGC90275.1, ECO:0000313|Proteomes:UP000006450};
RN   [1] {ECO:0000313|EMBL:EGC90275.1, ECO:0000313|Proteomes:UP000006450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HGA1 {ECO:0000313|EMBL:EGC90275.1,
RC   ECO:0000313|Proteomes:UP000006450};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Nelson K.E.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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:EGC90275.1}.
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DR   EMBL; AEXR01000008; EGC90275.1; -; Genomic_DNA.
DR   RefSeq; WP_009608149.1; NZ_AEXR01000008.1.
DR   AlphaFoldDB; F0HKL6; -.
DR   Proteomes; UP000006450; Unassembled WGS sequence.
DR   GO; GO:0018818; F:acetylene hydratase activity; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd02781; MopB_CT_Acetylene-hydratase; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 2.
DR   Gene3D; 2.20.25.90; ADC-like domains; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR037949; MopB_CT_Acetylene-hydratase.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 1.
DR   PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SMART; SM00926; Molybdop_Fe4S4; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1002
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003253573"
FT   DOMAIN          47..104
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   1002 AA;  112510 MW;  6218C09D5FA34093 CRC64;
     MGKTTVTRRA FAQLAAATGA IAAMGVGTRP AVALTDGNSG TAGERGIKKI RSCCRGCGKV
     ECGVWVYIQD GKVVRTEGDE TCFNTMGNHC SKGQASIQAA YHPDRIKFPM KRTNPKGSED
     PGWVRISWDE AYRTIADNIM QLREKYGPES LFTWCGTGRQ WCMQSDAGMA LELFGTPNII
     AAYQVCKGPR HFSSRLDNVQ AWSWSEVINH STKYVQWATD PSVSNYDDSS RLVIDVAREA
     EAFIVVDPRL SNLGRTAKYW LNLRPGTDNA MALGWCHIIL KHDLVDWQFV KRWSNASFIV
     VPDMDPSGYT EAVQNTKSPY EYRTRLLTEA DIDPSMVDWE IEGEGNPKRY LVYDQINRRW
     TYWQADPEDA HWEGETWTKQ TSGFTQDVSR LRDDESKVAG WIADLSEFDP RIDPALTGEF
     EVRLKDGSTH IGRPAWDLWA EYLQQFTPER VSEITGVDAQ LIEDAVVEWA TRDDPRIPNG
     GINYGLGVEH AGNSTQNCRA IMAACAMVGA IDTPGGQRGA TNGWTEQSGP CAMLPSMAAF
     AFMPTPDLSL KMAGNEKMPL LYWYGVWCDA NAAMECAHKE PDAPYEIHGG MIGSGDHMNM
     GNATYNWEAL NMLDFLFEAN LWHSPTSGAA DILLPVCHWT EINAYRIAQG ASGGFGLCVK
     AVDPPGECKS DPLYFMELSK YFGVPAFDGD DPWLENKPDA DLEIENLTIQ CCVQGCAPYN
     NWNELEAAFQ EHGWWNMKRE IPEDWGTYRR YEVGQAYRLA PHQQPAQLNI NKPGFPTPTM
     KHEFWCTSIE SFFPEGADGP ELAPGFTSEA LPYYAEPAHG PVVDAETYKE YPITCITGRR
     IPVYFHSEHR QLPWCRELWP VPRMEINPDT AAELGLEQGD WAWIESPWGK VRQTVDLYYG
     IKPNMINAEH QWWYPELAQA DKGYELSCIN CITDRKTQDK YNGSSNVRTY PVKVYKATPE
     NSPFGNPIPC GNDGTEIIHD SSDPRLKLWE IGAAGIHPDH FE
//
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