ID NIRT_STUST Reviewed; 201 AA. AC P24038; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-1992, sequence version 1. DT 24-JAN-2024, entry version 110. DE RecName: Full=Denitrification system component NirT; GN Name=nirT; OS Stutzerimonas stutzeri (Pseudomonas stutzeri). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Stutzerimonas. OX NCBI_TaxID=316; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 14405 / JCM 20778 / CIP 107696 / IAM 12931 / LMG 2243 / RC NCIMB 568 / Baumann 218 / ZoBell 632; RX PubMed=2001732; DOI=10.1016/0014-5793(91)80150-2; RA Juengst A., Wakabayashi S., Matsubara H., Zumft W.G.; RT "The nirSTBM region coding for cytochrome cd1-dependent nitrite respiration RT of Pseudomonas stutzeri consists of a cluster of mono-, di-, and tetraheme RT proteins."; RL FEBS Lett. 279:205-209(1991). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- INDUCTION: By anaerobic conditions. CC -!- PTM: Binds 4 heme groups per subunit. CC -!- SIMILARITY: Belongs to the NapC/NirT/NrfH family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X53676; CAA40151.1; -; Genomic_DNA. DR PIR; S13937; O4PSZ. DR RefSeq; WP_003279943.1; NZ_POUM01000011.1. DR AlphaFoldDB; P24038; -. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019333; P:denitrification pathway; IEA:InterPro. DR Gene3D; 1.10.3820.10; Di-heme elbow motif domain; 1. DR InterPro; IPR036280; Multihaem_cyt_sf. DR InterPro; IPR024717; NapC/NirT/NrfH. DR InterPro; IPR005126; NapC/NirT_cyt_c_N. DR InterPro; IPR038266; NapC/NirT_cytc_sf. DR InterPro; IPR011885; NO3Rdtase_cyt_c_NapC/NirT. DR NCBIfam; TIGR02161; napC_nirT; 1. DR PANTHER; PTHR30333; CYTOCHROME C-TYPE PROTEIN; 1. DR PANTHER; PTHR30333:SF1; CYTOCHROME C-TYPE PROTEIN NAPC; 1. DR Pfam; PF03264; Cytochrom_NNT; 1. DR PIRSF; PIRSF000013; 4_hem_cytochrm_NapC; 1. DR SUPFAM; SSF48695; Multiheme cytochromes; 1. DR PROSITE; PS51008; MULTIHEME_CYTC; 1. PE 2: Evidence at transcript level; KW Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..201 FT /note="Denitrification system component NirT" FT /id="PRO_0000108438" FT TOPO_DOM 1..24 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 25..45 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 46..201 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT BINDING 58 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="1" FT /note="covalent" FT /evidence="ECO:0000250|UniProtKB:Q72EF4" FT BINDING 61 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="1" FT /note="covalent" FT /evidence="ECO:0000250|UniProtKB:Q72EF4" FT BINDING 64 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="1" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:Q72EF4" FT BINDING 88 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="2" FT /note="covalent" FT /evidence="ECO:0000250|UniProtKB:Q72EF4" FT BINDING 91 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="2" FT /note="covalent" FT /evidence="ECO:0000250|UniProtKB:Q72EF4" FT BINDING 92 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="2" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:Q72EF4" FT BINDING 104 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q72EF4" FT BINDING 110 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="1" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:Q72EF4" FT BINDING 148 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="3" FT /note="covalent" FT /evidence="ECO:0000250|UniProtKB:Q72EF4" FT BINDING 151 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="3" FT /note="covalent" FT /evidence="ECO:0000250|UniProtKB:Q72EF4" FT BINDING 152 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="3" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:Q72EF4" FT BINDING 180 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="4" FT /note="covalent" FT /evidence="ECO:0000250|UniProtKB:Q72EF4" FT BINDING 183 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="4" FT /note="covalent" FT /evidence="ECO:0000250|UniProtKB:Q72EF4" FT BINDING 184 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="4" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:Q72EF4" FT BINDING 189 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="2" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:Q72EF4" FT SITE 175 FT /note="Interaction with NrfA" FT /evidence="ECO:0000250|UniProtKB:Q72EF4" SQ SEQUENCE 201 AA; 22825 MW; 68B20780C422A450 CRC64; MTDKDGNKQQ KGGILALLRR PSTRYSLGGI LIVGIVAGIV FWGGFNTALE ATNTETFCIS CHEMGDNVYP EYKETIHYAN RTGVRATCPD CHVPRDWTHK MVRKVEASKE LWGKIVGTID TAEKFEAKRL TLARREWARM RASDSRECRN CHSLESMSSD MQKQRARKQH EMAREDNLTC IACHKGIAHH LPEGMTEEDE D //