ID   H2B1_ICTPU              Reviewed;          21 AA.
AC   P81903;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Histone H2B 1;
DE   AltName: Full=Antibacterial histone-like protein 1;
DE            Short=HLP-1;
DE   Flags: Fragment;
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-21, FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Skin;
RX   PubMed=9645227; DOI=10.1007/s000180050175;
RA   Robinette D., Wada S., Arroll T., Levy M.G., Miller W.L., Noga E.J.;
RT   "Antimicrobial activity in the skin of the channel catfish Ictalurus
RT   punctatus: characterization of broad-spectrum histone-like antimicrobial
RT   proteins.";
RL   Cell. Mol. Life Sci. 54:467-475(1998).
CC   -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact
CC       DNA into chromatin, limiting DNA accessibility to the cellular
CC       machineries which require DNA as a template. Histones thereby play a
CC       central role in transcription regulation, DNA repair, DNA replication
CC       and chromosomal stability. DNA accessibility is regulated via a complex
CC       set of post-translational modifications of histones, also called
CC       histone code, and nucleosome remodeling. {ECO:0000269|PubMed:9645227}.
CC   -!- FUNCTION: Has broad-spectrum antimicrobial and antibacterial activity.
CC       It is important in the antimicrobial defenses of fish skin and
CC       possesses strong activity against saprolegnia, the most common fungal
CC       infection in fish. It is also inhibitory to fish bacterial pathogens,
CC       such as aeromonas hydrophila, vibrio alginolyticus and E.coli D31.
CC       {ECO:0000269|PubMed:9645227}.
CC   -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules
CC       each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and
CC       two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of
CC       DNA.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- PTM: Monoubiquitination at the C-terminal Lys gives a specific tag for
CC       epigenetic transcriptional activation and is also prerequisite for
CC       histone H3 'Lys-4' and 'Lys-79' methylation.
CC       {ECO:0000250|UniProtKB:P33778}.
CC   -!- PTM: Phosphorylated during apoptosis; which facilitates apoptotic
CC       chromatin condensation. {ECO:0000250|UniProtKB:P06900}.
CC   -!- MASS SPECTROMETRY: Mass=13459; Method=MALDI; Note=The measured range is
CC       2-21.; Evidence={ECO:0000269|PubMed:9645227};
CC   -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
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DR   Proteomes; UP000221080; Genome assembly.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IDA:AgBase.
DR   GO; GO:0050832; P:defense response to fungus; IDA:AgBase.
DR   GO; GO:0045087; P:innate immune response; IDA:AgBase.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Acetylation; Antibiotic; Antimicrobial; Chromosome;
KW   Direct protein sequencing; DNA-binding; Fungicide; Isopeptide bond;
KW   Nucleosome core; Nucleus; Phosphoprotein; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9645227"
FT   CHAIN           2..>21
FT                   /note="Histone H2B 1"
FT                   /id="PRO_0000071849"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         6
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1H4"
FT   MOD_RES         11
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1H4"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P06900"
FT   MOD_RES         14
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1H4"
FT   MOD_RES         19
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1H4"
FT   CROSSLNK        19
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1H4"
FT   NON_TER         21
SQ   SEQUENCE   21 AA;  2166 MW;  C13E4A04853CA66F CRC64;
     MPDPAKTAPK KGSKKAVTKX A