ID Q7MSJ8_WOLSU Unreviewed; 702 AA. AC Q7MSJ8; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 15-DEC-2003, sequence version 1. DT 01-APR-2015, entry version 55. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:CAE09526.1}; GN OrderedLocusNames=WS0379 {ECO:0000313|EMBL:CAE09526.1}; OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC OS 11488 / FDC 602W) (Vibrio succinogenes). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Wolinella. OX NCBI_TaxID=273121 {ECO:0000313|Proteomes:UP000000422}; RN [1] {ECO:0000313|Proteomes:UP000000422} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W RC {ECO:0000313|Proteomes:UP000000422}; RX PubMed=14500908; DOI=10.1073/pnas.1932838100; RA Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O., RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B., RA Meyer F., Lederer H., Schuster S.C.; RT "Complete genome sequence and analysis of Wolinella succinogenes."; RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003). 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; BX571658; CAE09526.1; -; Genomic_DNA. DR RefSeq; NP_906626.1; NC_005090.1. DR RefSeq; WP_011138326.1; NC_005090.1. DR PDB; 4RKM; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=1-702. DR PDB; 4RKN; X-ray; 2.10 A; A/B/C/D=1-702. DR ProteinModelPortal; Q7MSJ8; -. DR STRING; 273121.WS0379; -. DR EnsemblBacteria; CAE09526; CAE09526; WS0379. DR KEGG; wsu:WS0379; -. DR PATRIC; 24037854; VBIWolSuc63014_0363. DR HOGENOM; HOG000286693; -. DR OMA; EHPEVDN; -. DR OrthoDB; EOG6T4RVP; -. DR Proteomes; UP000000422; Chromosome. DR Gene3D; 1.10.710.10; -; 2. DR InterPro; IPR023155; Cyt_c-552/4. DR InterPro; IPR029467; Cytochrome_c3/c7. DR InterPro; IPR011031; Multihaem_cyt. DR Pfam; PF14522; Cytochrome_C7; 1. DR PROSITE; PS51008; MULTIHEME_CYTC; 2. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:4RKM, ECO:0000213|PDB:4RKN}; KW Complete proteome {ECO:0000313|Proteomes:UP000000422}; KW Heme {ECO:0000213|PDB:4RKM, ECO:0000213|PDB:4RKN}; KW Iron {ECO:0000213|PDB:4RKM, ECO:0000213|PDB:4RKN}; KW Metal-binding {ECO:0000213|PDB:4RKM, ECO:0000213|PDB:4RKN}; KW Reference proteome {ECO:0000313|Proteomes:UP000000422}. FT METAL 159 159 Iron (heme 1 axial ligand); via tele FT nitrogen. {ECO:0000213|PDB:4RKM, FT ECO:0000213|PDB:4RKN}. FT METAL 159 159 Iron (heme 4 axial ligand); via tele FT nitrogen. {ECO:0000213|PDB:4RKM}. FT METAL 171 171 Iron (heme 6 axial ligand); via tele FT nitrogen. {ECO:0000213|PDB:4RKM, FT ECO:0000213|PDB:4RKN}. FT METAL 318 318 Iron (heme 3 axial ligand); via tele FT nitrogen. {ECO:0000213|PDB:4RKM, FT ECO:0000213|PDB:4RKN}. FT METAL 355 355 Iron (heme 5 axial ligand); via tele FT nitrogen. {ECO:0000213|PDB:4RKM, FT ECO:0000213|PDB:4RKN}. FT METAL 360 360 Iron (heme 1 axial ligand); via tele FT nitrogen. {ECO:0000213|PDB:4RKM, FT ECO:0000213|PDB:4RKN}. FT METAL 360 360 Iron (heme 4 axial ligand); via tele FT nitrogen. {ECO:0000213|PDB:4RKM}. FT METAL 376 376 Iron (heme 6 axial ligand); via tele FT nitrogen. {ECO:0000213|PDB:4RKM, FT ECO:0000213|PDB:4RKN}. FT METAL 423 423 Iron (heme 8 axial ligand); via tele FT nitrogen. {ECO:0000213|PDB:4RKM, FT ECO:0000213|PDB:4RKN}. FT METAL 434 434 Iron (heme 7 axial ligand); via tele FT nitrogen. {ECO:0000213|PDB:4RKM, FT ECO:0000213|PDB:4RKN}. FT METAL 437 437 Iron (heme 5 axial ligand); via tele FT nitrogen. {ECO:0000213|PDB:4RKM, FT ECO:0000213|PDB:4RKN}. FT METAL 478 478 Iron (heme 8 axial ligand); via tele FT nitrogen. {ECO:0000213|PDB:4RKM, FT ECO:0000213|PDB:4RKN}. FT METAL 491 491 Iron (heme 10 axial ligand); via tele FT nitrogen. {ECO:0000213|PDB:4RKM, FT ECO:0000213|PDB:4RKN}. FT METAL 500 500 Iron (heme 9 axial ligand); via tele FT nitrogen. {ECO:0000213|PDB:4RKM, FT ECO:0000213|PDB:4RKN}. FT METAL 528 528 Iron (heme 7 axial ligand); via tele FT nitrogen. {ECO:0000213|PDB:4RKM, FT ECO:0000213|PDB:4RKN}. FT METAL 591 591 Iron (heme 10 axial ligand); via tele FT nitrogen. {ECO:0000213|PDB:4RKM, FT ECO:0000213|PDB:4RKN}. FT METAL 675 675 Iron (heme 9 axial ligand); via tele FT nitrogen. {ECO:0000213|PDB:4RKM, FT ECO:0000213|PDB:4RKN}. FT BINDING 155 155 Heme 1 (covalent). {ECO:0000213|PDB: FT 4RKN}. FT BINDING 351 351 Heme 5 (covalent). {ECO:0000213|PDB:4RKM, FT ECO:0000213|PDB:4RKN}. FT BINDING 372 372 Heme 6 (covalent). {ECO:0000213|PDB: FT 4RKN}. FT BINDING 375 375 Heme 6 (covalent). {ECO:0000213|PDB: FT 4RKN}. FT BINDING 430 430 Heme 7 (covalent). {ECO:0000213|PDB:4RKM, FT ECO:0000213|PDB:4RKN}. FT BINDING 474 474 Heme 8 (covalent). {ECO:0000213|PDB:4RKM, FT ECO:0000213|PDB:4RKN}. FT BINDING 496 496 Heme 9 (covalent). {ECO:0000213|PDB:4RKM, FT ECO:0000213|PDB:4RKN}. FT BINDING 574 574 Heme 10 (covalent). {ECO:0000213|PDB: FT 4RKN}. FT DISULFID 411 507 {ECO:0000213|PDB:4RKN}. SQ SEQUENCE 702 AA; 78939 MW; 7F03B02298162E28 CRC64; MLSGWSVLKG GNMKYWDKAL LSLFMCVSTL SIAATHAVAM EGMQMTKEAR EIIAHPKGTK ESRGVISLQD YIVEEQAMYD WLFKNHPIFT KYGGKTVGKL VVKDRGEEWI EEGRGNDFSK ASKRSGGEGF SSMMYRVARN STLQYPNKFI GPEKCGECHP AQYETWSRSR HATTIRFPGE HPEVNNKLND PVFDKDTASI LPQGITPDVV YCTVGHIRTK FGFFDAWLLR GTYHVEGGLL KNGTGQIVAG GNQWQRTWAL NLSPEVAKKI KKWVPDFPVT LEEYGDNGGY VRGLASYAAK YKKSMSFQAS TSYCEVCHPW KFDFKNESEF YAALGNAKEL QKHTISKGVS CEECHGAGGH LEGGSGLLIS NCERCHQRFS YSPDLMRNNP LNAGKPDLAL SSKFKSMGPG CGSEGSQTYF TAHYEKGMRC ATCHDPHDVT GNVTGEKGIK GVSYNSEQGY LSSLYSKPKL KKECTDCHKE QAYIQSKADT HSKNSCASCH MPFMMSCENF YAIQFQDQAG FDTQRRAHIW KIDVDPARKS LVAGSTSKDP RDGKDWHFER NEEGRNFVDL MWACARTTWA DKDQAEAKGC HSPVVSELKE TLHFKDQKQV YNEVMGWQTP VKDKFTQVKV GIQGLYSLLE VKKLAPSDKT RVYELIEKAQ DTVDLIEKDG SWGMHGFKYT KQRLDAAVEY INEAQRIMKK SL //