Belongs to the RNA polymerase beta chain family.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription.
In elementary bodies (EBs, the infectious stage, which is able to survive outside the host cell) provides the structural integrity of the outer envelope through disulfide cross-links with the large cysteine-rich periplasmic protein and the major outer membrane porin. It has been described in publications as the Sarkosyl-insoluble COMC (Chlamydia outer membrane complex), and serves as the functional equivalent of peptidoglycan.
N-terminal amide-linked and S-diacylglycerol cysteine-linked to 16:0, 18:0, 15:0 branched, and 17:0 branched fatty acids (ratio 6:5:3:4) in the EB stage (PubMed:7928970). The exact distribution of fatty acids has not been determined.
Part of a disulfide cross-linked outer membrane complex (COMC) composed of the major outer membrane porin (MOMP), the small cysteine-rich protein (omcA) and the large cysteine-rich periplasmic protein (omcB).
Belongs to the chlamydial porin (CP) (TC 1.B.2) family.
In elementary bodies (EBs, the infectious stage, which is able to survive outside the host cell) provides the structural integrity of the outer envelope through disulfide cross-links with the small cysteine-rich protein and the large cysteine-rich periplasmic protein. It has been described in publications as the Sarkosyl-insoluble COMC (Chlamydia outer membrane complex), and serves as the functional equivalent of peptidoglycan. It is present but some of the disulfide bonds are reduced in reticulate bodies (RBs).
Permits diffusion of specific solutes through the outer membrane.
Preferentially transcribed early during the life cycle.
Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Belongs to the universal ribosomal protein uL22 family.
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.
This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g., L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.
Belongs to the universal ribosomal protein uL4 family.
Forms part of the polypeptide exit tunnel.
One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.
Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. RsmA subfamily.
Lacks conserved residue(s) required for the propagation of feature annotation.
Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
In elementary bodies (EBs, the infectious stage, which is able to survive outside the host cell) provides the structural integrity of the outer envelope through disulfide cross-links with the small cysteine-rich protein and the major outer membrane porin. It has been described in publications as the Sarkosyl-insoluble COMC (Chlamydia outer membrane complex), and serves as the functional equivalent of peptidoglycan.
Was thought to be an outer membrane protein as it is part of a disulfide cross-linked complex that is insoluble in the detergent Sarkosyl. In PubMed:7532170 it was shown to likely be periplasmic.