ID A0A2S2FBL9_9GAMM Unreviewed; 877 AA.
AC A0A2S2FBL9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=PepSY domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=DJ533_06745 {ECO:0000313|EMBL:AWL28288.1};
OS Acinetobacter defluvii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1871111 {ECO:0000313|EMBL:AWL28288.1, ECO:0000313|Proteomes:UP000245977};
RN [1] {ECO:0000313|Proteomes:UP000245977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCHA30 {ECO:0000313|Proteomes:UP000245977};
RA Hu Y., Qin J., Feng Y., Zong Z.;
RT "The complete genome of Acinetobacter defluvii strain WCHAD010030.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP029397; AWL28288.1; -; Genomic_DNA.
DR RefSeq; WP_065993616.1; NZ_CP029397.2.
DR AlphaFoldDB; A0A2S2FBL9; -.
DR STRING; 1871111.GCA_001704615_02843; -.
DR KEGG; adv:DJ533_06745; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000245977; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd06200; SiR_like1; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR005625; PepSY-ass_TM.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR34219:SF3; BLL7967 PROTEIN; 1.
DR PANTHER; PTHR34219; IRON-REGULATED INNER MEMBRANE PROTEIN-RELATED; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF03929; PepSY_TM; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 4: Predicted;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000245977};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022982}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 371..395
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 423..561
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 575..738
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 230..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 877 AA; 100197 MW; DA3845559A275BE8 CRC64;
MFKKILFQLH WFFGITAGLI LSIMGVTGAI YSYEQPIQKW LNPDSYTVQV ENRAKLTPAE
IYQHFQITQP KIKINSITIH QAPDASSSIN IEKEGARKGF NVMINPYSAE ILPEVKGREF
FQFIQQLHRN LTVGPVGKQI TAACTLILIY FILSGLYLRW PKKHSFKQWF SIKPKLKGRN
FLWDLHAVVG TWVVIFYLLL AVTGLYWSYD WWRNGMFKVL GVDRPQPEMQ ANAGKAKQTE
QMRGAGTSAE QVRGEKTTSA NAEGHGKGRE QSKLDSKQIA LAYTQTWTGF HAQLKQDYSS
ITLSTPKKAD GTMDVSFVDA IPQHERARNK AIYNYQNNQI EKIELYADKK LNEKIMSSML
PVHRGSFFGP VYQFLVMLAA LSMPLFFVTG WMLYLKRRKQ KQLTLAARHH TAIIDVDPHA
TPWLISYASQ TGVSEQLTWR TATNLQAARQ PVTVKALQHL TIEDLQNCPQ ILFIVSTYGT
GEAPDLAITF VKKIMPHSFD LKHLKYAVLA LGSKEYPETY CSFGHWLDTW LQQNQAQAMF
NTIEVDNANA ADIEKWTTAL AKISKLELSH MHIEKVFDEW TFKKRELLNP NSLGGPVFNL
EFHTVHEVVW QAGDIAEIQP GNSLERILAF LDKYHIASNT PVNELNLTIQ QALWNRNLTV
EVEPFANMQH LLEQLPILPT REYSIASIPE QQVLRLVVRQ QSDTDGNLGL GSGWLTQHTQ
VSEQIAMRIR TNPSFHLIND NRPIICIGNG TGIAGLMSLI HARVRLNYTE NWLIFGERQQ
AHDFFFKETL EAWQTTGMLK RLDLAFSRDQ AEKNYVHHKL HEQQDLLKTW ITQGAVIYVC
GSIQGMASDV DHALVEILGE TQLNQLRENG RYKRDVY
//
