ID   O05192_KLEPN            Unreviewed;       379 AA.
AC   O05192;
DT   01-JUL-1997, integrated into UniProtKB/TrEMBL.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Subunit II of cytochrome bd {ECO:0000313|EMBL:CAA71118.1};
GN   Name=cydB {ECO:0000313|EMBL:CAA71118.1};
OS   Klebsiella pneumoniae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573 {ECO:0000313|EMBL:CAA71118.1};
RN   [1] {ECO:0000313|EMBL:CAA71118.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=M5a1 {ECO:0000313|EMBL:CAA71118.1};
RA   Merrick M.J.;
RL   Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAA71118.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=M5a1 {ECO:0000313|EMBL:CAA71118.1};
RX   PubMed=9274021;
RA   Juty N.S., Moshiri F., Merrick M., Anthony C., Hill S.;
RT   "The Klebsiella pneumoniae cytochrome bd terminal oxidase complex and its
RT   role in microaerobic nitrogen fixation.";
RL   Microbiology 143:2673-2683(1997).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the cytochrome ubiquinol oxidase subunit 2
CC       family. {ECO:0000256|ARBA:ARBA00007543}.
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DR   EMBL; Y10012; CAA71118.1; -; Genomic_DNA.
DR   AlphaFoldDB; O05192; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR003317; Cyt-d_oxidase_su2.
DR   NCBIfam; TIGR00203; cydB; 1.
DR   PANTHER; PTHR43141:SF5; CYTOCHROME BD-I UBIQUINOL OXIDASE SUBUNIT 2; 1.
DR   PANTHER; PTHR43141; CYTOCHROME BD2 SUBUNIT II; 1.
DR   Pfam; PF02322; Cyt_bd_oxida_II; 1.
DR   PIRSF; PIRSF000267; Cyt_oxidse_sub2; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        6..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        78..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        119..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        161..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        203..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        264..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        290..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        335..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   379 AA;  42398 MW;  252F1B835E5603E7 CRC64;
     MIDYEVLRFI WWLLIGILLI GFAVADGFDM GVGMLTRFLG RNDTERRIMI NAIAPHWDGN
     QVWLITAGGA LFAAWPMVYA AAFSGFYVAM ILVLASLFFR PVGFDYRSKI EDNRWRNMWD
     WGIFVGSFVP PLVIGVAFGN LLQGVPFHVD EYLRLYYTGN FFQLLNPFGL LAGIVSVAMI
     LTQGATYLQM RTVGELHLRT RSVSTVPALV TLICFALAGV WVYYGIDGYV VKSVMDHTGP
     SNPLTKEVAR EAGAWMVNFN NMPALWAIPA LGPWLPLLTV ISTKADKGAW AFLFSSLTLA
     CIILTAGIAM FPFIMPSSTA MNASLTMWDA TSSTLTLNVM TYVAIVFVPI ILAYTTWCYW
     KMFGRITRED IEKNTHSLY
//