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Database: UniProt
Entry: A0A2C6DNE5_9GAMM
LinkDB: A0A2C6DNE5_9GAMM
Original site: A0A2C6DNE5_9GAMM 
ID   A0A2C6DNE5_9GAMM        Unreviewed;       166 AA.
AC   A0A2C6DNE5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Ferredoxin-type protein NapF {ECO:0000256|HAMAP-Rule:MF_02201};
GN   Name=napF {ECO:0000256|HAMAP-Rule:MF_02201,
GN   ECO:0000313|EMBL:PHI31858.1};
GN   ORFNames=CRN84_22325 {ECO:0000313|EMBL:PHI31858.1}, NCTC12282_06081
GN   {ECO:0000313|EMBL:VFS52873.1};
OS   Budvicia aquatica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Budviciaceae; Budvicia.
OX   NCBI_TaxID=82979 {ECO:0000313|EMBL:PHI31858.1, ECO:0000313|Proteomes:UP000224974};
RN   [1] {ECO:0000313|EMBL:PHI31858.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FDAARGOS_387 {ECO:0000313|EMBL:PHI31858.1};
RA   Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.J.,
RA   Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA   Nadendla S., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx tests.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000224974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FDAARGOS_387 {ECO:0000313|Proteomes:UP000224974};
RA   Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA   Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA   Nadendla S., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx tests.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:VFS52873.1, ECO:0000313|Proteomes:UP000373449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC12282 {ECO:0000313|EMBL:VFS52873.1,
RC   ECO:0000313|Proteomes:UP000373449};
RG   Pathogen Informatics;
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Could be involved in the maturation of NapA, the catalytic
CC       subunit of the periplasmic nitrate reductase, before its export into
CC       the periplasm. {ECO:0000256|HAMAP-Rule:MF_02201}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02201};
CC   -!- SUBUNIT: Interacts with the cytoplasmic NapA precursor.
CC       {ECO:0000256|HAMAP-Rule:MF_02201}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02201}.
CC   -!- SIMILARITY: Belongs to the NapF family. {ECO:0000256|HAMAP-
CC       Rule:MF_02201}.
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DR   EMBL; PDDX01000001; PHI31858.1; -; Genomic_DNA.
DR   EMBL; CAADJA010000002; VFS52873.1; -; Genomic_DNA.
DR   RefSeq; WP_029096777.1; NZ_PDDX01000001.1.
DR   AlphaFoldDB; A0A2C6DNE5; -.
DR   STRING; 1111728.GCA_000427805_03254; -.
DR   OrthoDB; 9808559at2; -.
DR   Proteomes; UP000224974; Unassembled WGS sequence.
DR   Proteomes; UP000373449; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd10564; NapF_like; 1.
DR   Gene3D; 3.30.70.20; -; 2.
DR   HAMAP; MF_02201; NapF; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004496; NapF.
DR   NCBIfam; TIGR00402; napF; 1.
DR   PANTHER; PTHR43687; ADENYLYLSULFATE REDUCTASE, BETA SUBUNIT; 1.
DR   PANTHER; PTHR43687:SF4; BLR5484 PROTEIN; 1.
DR   Pfam; PF12838; Fer4_7; 2.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 3.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_02201};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02201};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_02201};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW   Rule:MF_02201};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_02201}; Reference proteome {ECO:0000313|Proteomes:UP000224974};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_02201}.
FT   DOMAIN          22..55
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          56..87
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          130..159
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   BINDING         35
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02201"
FT   BINDING         38
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02201"
FT   BINDING         41
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02201"
FT   BINDING         45
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02201"
FT   BINDING         67
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02201"
FT   BINDING         70
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02201"
FT   BINDING         73
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02201"
FT   BINDING         77
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02201"
FT   BINDING         139
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02201"
FT   BINDING         142
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02201"
FT   BINDING         145
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02201"
FT   BINDING         149
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02201"
SQ   SEQUENCE   166 AA;  18183 MW;  315F9A8DCF4AB484 CRC64;
     MSVLSRRNLL RGQWHRSSAI RPPWSIDEAQ FIDGCTRCHA CVDACETQVL IVKGEGFPEI
     DFQRAECTFC GRCVAACPEP VFTSIQNQPW QRKAVISTTC LTFQNVACRS CQDVCEPNAI
     KFKLRLGGIA QPELDSDSCT GCGSCISSCP VQAITTSESD KDNVGK
//
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