ID   H2B_PENVA               Reviewed;         116 AA.
AC   P83863;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Histone H2B;
DE   Flags: Fragments;
OS   Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC   Penaeoidea; Penaeidae; Penaeus.
OX   NCBI_TaxID=6689;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, MASS SPECTROMETRY, AND ACETYLATION AT LYS-4; LYS-11 AND
RP   LYS-14.
RC   TISSUE=Hemocyte {ECO:0000269|PubMed:17405180};
RX   PubMed=17405180; DOI=10.1002/jms.1200;
RA   Ouvry-Patat S.A., Schey K.L.;
RT   "Characterization of antimicrobial histone sequences and posttranslational
RT   modifications by mass spectrometry.";
RL   J. Mass Spectrom. 42:664-674(2007).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 49-63 AND 75-112, FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Hemocyte {ECO:0000269|PubMed:15606770};
RX   PubMed=15606770; DOI=10.1111/j.1432-1033.2004.04448.x;
RA   Patat S.A., Carnegie R.B., Kingsbury C., Gross P.S., Chapman R.,
RA   Schey K.L.;
RT   "Antimicrobial activity of histones from hemocytes of the Pacific white
RT   shrimp.";
RL   Eur. J. Biochem. 271:4825-4833(2004).
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:15606770}.
CC   -!- FUNCTION: A mixture of histones H2B and H4 has antimicrobial activity
CC       against the Gram-positive bacterium M.luteus.
CC       {ECO:0000269|PubMed:15606770}.
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. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome.
CC   -!- PTM: Monoubiquitination gives a specific tag for epigenetic
CC       transcriptional activation and is also prerequisite for histone H3
CC       'Lys-4' and 'Lys-79' methylation. {ECO:0000250|UniProtKB:P33778}.
CC   -!- PTM: GlcNAcylation at Ser-103 promotes monoubiquitination of Lys-111.
CC       It fluctuates in response to extracellular glucose, and associates with
CC       transcribed genes (By similarity). {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=13554; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15606770};
CC   -!- MASS SPECTROMETRY: Mass=13570; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:17405180};
CC   -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000255}.
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DR   AlphaFoldDB; P83863; -.
DR   SMR; P83863; -.
DR   iPTMnet; P83863; -.
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:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0044877; F:protein-containing complex binding; ISS:UniProtKB.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
DR   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR007125; Histone_H2A/H2B/H3.
DR   InterPro; IPR000558; Histone_H2B.
DR   PANTHER; PTHR23428; PTHR23428; 1.
DR   Pfam; PF00125; Histone; 1.
DR   PRINTS; PR00621; HISTONEH2B.
DR   SMART; SM00427; H2B; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
DR   PROSITE; PS00357; HISTONE_H2B; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Antibiotic; Antimicrobial; Chromosome;
KW   Direct protein sequencing; DNA-binding; Glycoprotein; Isopeptide bond;
KW   Nucleosome core; Nucleus; Ubl conjugation.
FT   CHAIN           <1..116
FT                   /note="Histone H2B"
FT                   /id="PRO_0000071878"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         4
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:17405180"
FT   MOD_RES         11
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:17405180"
FT   MOD_RES         14
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:17405180"
FT   CARBOHYD        103
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        111
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   NON_CONS        23..24
FT                   /evidence="ECO:0000303|PubMed:17405180"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:17405180"
SQ   SEQUENCE   116 AA;  12775 MW;  9D64B5450938D9A5 CRC64;
     TSGKAAKKAG KAQKSITKGD KKKRKESYSI YIYKVLKQVH PDTGISSKAM SIMNSFVNDI
     FERIAAEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT KYTSSK