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Database: UniProt
Entry: C6S7Z4_NEIML
LinkDB: C6S7Z4_NEIML
Original site: C6S7Z4_NEIML 
ID   C6S7Z4_NEIML            Unreviewed;       642 AA.
AC   C6S7Z4;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=RNA polymerase sigma factor RpoD {ECO:0000256|HAMAP-Rule:MF_00963};
DE   AltName: Full=Sigma-70 {ECO:0000256|HAMAP-Rule:MF_00963};
GN   Name=rpoD {ECO:0000256|HAMAP-Rule:MF_00963,
GN   ECO:0000313|EMBL:CBA06900.1};
GN   OrderedLocusNames=NMO_1358 {ECO:0000313|EMBL:CBA06900.1};
OS   Neisseria meningitidis (strain alpha14).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=662598 {ECO:0000313|EMBL:CBA06900.1, ECO:0000313|Proteomes:UP000002054};
RN   [1] {ECO:0000313|EMBL:CBA06900.1, ECO:0000313|Proteomes:UP000002054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=alpha14 {ECO:0000313|Proteomes:UP000002054};
RX   PubMed=18305155; DOI=10.1073/pnas.0800151105;
RA   Schoen C., Blom J., Claus H., Schramm-Glueck A., Brandt P., Mueller T.,
RA   Goesmann A., Joseph B., Konietzny S., Kurzai O., Schmitt C., Friedrich T.,
RA   Linke B., Vogel U., Frosch M.;
RT   "Whole-genome comparison of disease and carriage strains provides insights
RT   into virulence evolution in Neisseria meningitidis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:3473-3478(2008).
CC   -!- FUNCTION: Sigma factors are initiation factors that promote the
CC       attachment of RNA polymerase to specific initiation sites and are then
CC       released. This sigma factor is the primary sigma factor during
CC       exponential growth. {ECO:0000256|HAMAP-Rule:MF_00963}.
CC   -!- SUBUNIT: Interacts transiently with the RNA polymerase catalytic core.
CC       {ECO:0000256|HAMAP-Rule:MF_00963}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00963}.
CC   -!- SIMILARITY: Belongs to the sigma-70 factor family. RpoD/SigA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00963}.
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DR   EMBL; AM889136; CBA06900.1; -; Genomic_DNA.
DR   RefSeq; WP_002212852.1; NC_013016.1.
DR   AlphaFoldDB; C6S7Z4; -.
DR   GeneID; 61281715; -.
DR   KEGG; nmi:NMO_1358; -.
DR   HOGENOM; CLU_014793_7_0_4; -.
DR   Proteomes; UP000002054; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006352; P:DNA-templated transcription initiation; IEA:UniProtKB-UniRule.
DR   CDD; cd06171; Sigma70_r4; 1.
DR   Gene3D; 1.10.601.10; RNA Polymerase Primary Sigma Factor; 1.
DR   Gene3D; 1.10.220.120; Sigma-70 factor, region 1.1; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR   HAMAP; MF_00963; Sigma70_RpoD_SigA; 1.
DR   InterPro; IPR014284; RNA_pol_sigma-70_dom.
DR   InterPro; IPR000943; RNA_pol_sigma70.
DR   InterPro; IPR009042; RNA_pol_sigma70_r1_2.
DR   InterPro; IPR007627; RNA_pol_sigma70_r2.
DR   InterPro; IPR007624; RNA_pol_sigma70_r3.
DR   InterPro; IPR007630; RNA_pol_sigma70_r4.
DR   InterPro; IPR007631; RNA_pol_sigma_70_non-ess.
DR   InterPro; IPR007127; RNA_pol_sigma_70_r1_1.
DR   InterPro; IPR042189; RNA_pol_sigma_70_r1_1_sf.
DR   InterPro; IPR013325; RNA_pol_sigma_r2.
DR   InterPro; IPR013324; RNA_pol_sigma_r3/r4-like.
DR   InterPro; IPR012760; RNA_pol_sigma_RpoD_C.
DR   InterPro; IPR028630; Sigma70_RpoD.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   NCBIfam; TIGR02393; RpoD_Cterm; 1.
DR   NCBIfam; TIGR02937; sigma70-ECF; 1.
DR   PANTHER; PTHR30603; RNA POLYMERASE SIGMA FACTOR RPO; 1.
DR   PANTHER; PTHR30603:SF47; RNA POLYMERASE SIGMA FACTOR SIGF, CHLOROPLASTIC; 1.
DR   Pfam; PF04546; Sigma70_ner; 1.
DR   Pfam; PF03979; Sigma70_r1_1; 1.
DR   Pfam; PF00140; Sigma70_r1_2; 1.
DR   Pfam; PF04542; Sigma70_r2; 1.
DR   Pfam; PF04539; Sigma70_r3; 1.
DR   Pfam; PF04545; Sigma70_r4; 1.
DR   PRINTS; PR00046; SIGMA70FCT.
DR   SUPFAM; SSF88946; Sigma2 domain of RNA polymerase sigma factors; 1.
DR   SUPFAM; SSF88659; Sigma3 and sigma4 domains of RNA polymerase sigma factors; 2.
DR   PROSITE; PS00715; SIGMA70_1; 1.
DR   PROSITE; PS00716; SIGMA70_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00963};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00963};
KW   Sigma factor {ECO:0000256|ARBA:ARBA00023082, ECO:0000256|HAMAP-
KW   Rule:MF_00963};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00963};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW   Rule:MF_00963}.
FT   DOMAIN          427..440
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00715"
FT   DOMAIN          596..622
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00716"
FT   DNA_BIND        597..616
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          200..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          403..473
FT                   /note="Sigma-70 factor domain-2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          482..558
FT                   /note="Sigma-70 factor domain-3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          571..624
FT                   /note="Sigma-70 factor domain-4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   COILED          290..324
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          354..402
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           427..430
FT                   /note="Interaction with polymerase core subunit RpoC"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   COMPBIAS        212..228
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   642 AA;  73788 MW;  7796E947FC057458 CRC64;
     MSKNQNHEEY QDDARPLTIE EQRARLRQLI IMGKERGYIT YSEINDALPD DMSDADQIDN
     IVSMISGLGI QVTEHAPDAE DILLSDNAAV TDDDAVEEAE AALSSADSEF GRTTDPVRMY
     MREMGQVDLL TREDEIIIAK KIENALKNMV QAISACPGSI AEILELIEKI RKDEIRVDEV
     VEAIIDPNEV LLNELGLGHL ETTAPEKPSN DNSDENEDDE ESEEDADEIS AANLAELKQK
     VIGHFAQIEK DYKKMIGRLE KHHSRHKDYL AYRDAIANKL LEVRFATRQI DSLSSSLRGK
     VENIRKLERE IRDICLDRVH MERDYFIQNF LPEITNLEWI EEEIAKGRVW SDALDRFRHA
     ILEKQTELAD MEKETRISIE ELKEINKNMV SSEKETAAAK QEMIQANLRL VISIAKKYTN
     RGLQFLDLIQ EGNIGLMKAV DKFEYRRGYK FSTYATWWIR QAITRSIADQ ARTIRIPVHM
     IETINKMNRI SRQHLQETGE EPDSAKLAEL MQMPEDKIRK IMKIAKEPIS METPIGDDDD
     SHLGDFIEDA NNVAPADAAM YTSLHEVTKE ILESLTPREA KVLRMRFGID MNTDHTLEEV
     GRQFDVTRER IRQIEAKALR KLRHPTRSDR LRSFLDSEDS KL
//
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