ID   HMW2_MYCPN              Reviewed;        1818 AA.
AC   P75471;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Cytadherence high molecular weight protein 2;
DE   AltName: Full=Cytadherence accessory protein 2;
GN   Name=hmw2; OrderedLocusNames=MPN_310; ORFNames=MP526;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=9098066; DOI=10.1128/jb.179.8.2668-2677.1997;
RA   Krause D.C., Proft T., Hedreyda C.T., Hilbert H., Plagens H., Herrmann R.;
RT   "Transposon mutagenesis reinforces the correlation between Mycoplasma
RT   pneumoniae cytoskeletal protein HMW2 and cytadherence.";
RL   J. Bacteriol. 179:2668-2677(1997).
RN   [3]
RP   PHOSPHORYLATION.
RX   PubMed=7635846; DOI=10.1128/jb.177.15.4571-4574.1995;
RA   Krebes K.A., Dirksen L.B., Krause D.C.;
RT   "Phosphorylation of Mycoplasma pneumoniae cytadherence-accessory proteins
RT   in cell extracts.";
RL   J. Bacteriol. 177:4571-4574(1995).
CC   -!- FUNCTION: Component of the cytoskeleton-like structure which stabilizes
CC       the shape of the wall-less Mycoplasma. This cytoskeleton-like network
CC       of accessory proteins containing HMW proteins 1 to 5 allows the proper
CC       anchoring of cytadhesin proteins in the mycoplasmal membrane at the
CC       attachment organelle (By similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylated mainly on serine residues.
CC       {ECO:0000269|PubMed:7635846}.
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DR   EMBL; U00089; AAB96174.1; -; Genomic_DNA.
DR   EMBL; U59896; AAB52527.1; -; Genomic_DNA.
DR   PIR; S73852; S73852.
DR   RefSeq; NP_109998.1; NC_000912.1.
DR   RefSeq; WP_010874666.1; NC_000912.1.
DR   AlphaFoldDB; P75471; -.
DR   SMR; P75471; -.
DR   IntAct; P75471; 1.
DR   STRING; 272634.MPN_310; -.
DR   PRIDE; P75471; -.
DR   EnsemblBacteria; AAB96174; AAB96174; MPN_310.
DR   KEGG; mpn:MPN_310; -.
DR   PATRIC; fig|272634.6.peg.334; -.
DR   HOGENOM; CLU_237675_0_0_14; -.
DR   OMA; KHDRQQA; -.
DR   BioCyc; MPNE272634:G1GJ3-494-MON; -.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0020035; P:adhesion of symbiont to microvasculature; IEA:UniProtKB-KW.
DR   InterPro; IPR016430; Cytadherence_Hmw2.
DR   PIRSF; PIRSF004800; Hmw2; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytadherence; Phosphoprotein; Reference proteome; Virulence.
FT   CHAIN           1..1818
FT                   /note="Cytadherence high molecular weight protein 2"
FT                   /id="PRO_0000084014"
FT   COILED          31..880
FT                   /evidence="ECO:0000255"
FT   COILED          919..1607
FT                   /evidence="ECO:0000255"
FT   COILED          1644..1755
FT                   /evidence="ECO:0000255"
FT   COILED          1786..1817
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1818 AA;  215622 MW;  66DF4B08F0FCFBC0 CRC64;
     MNDTDKKFPL QPVYDTGFDD GYLQRDYEKC LESAAANDAQ TVELQTQLLA EIKNLENEIK
     ALKAQESRQP DPHNNARIQS LEASLNRLVN EYNNFEFQKN YMVDRVAELN NKARFFKDEL
     KRLQQENAAF VNSRYANWAD FQSNYQLKLD QFQALIDQQN QTIKQLNEQI AANQGLIDQN
     VQRLQQNHSL DQQERDALLY EVDHLYNELY ELENQKRLVG IEYEATYQDL VSADAELQNV
     YETIAQNQAN FQKQCDAYWA QLKQVEQQIQ TTKQELVDEE STLKVRLNDA DFYINSRLAE
     LDDLTSKINE RDFVSKEQAQ DVKASLANLT KEKERLSAEK DSFERLRNTA LNDINRMEQE
     NALFAKHLEQ QQYEFERKQQ ESLLKLETEH KQLQKRIGEF KIESEAKSEA LLIQERELLE
     KRREIDDLLT QASLEYEQQR RTNQVLKEKH RQVQQHFQNL VHAKKKLDQK RHYLAEQKRI
     DEEQIFKLKE KIATERRELE KLYLVKKQKQ DQKENDLLIF EKQLRQYQAD FENEIEEKQN
     ELFASQKSLQ KSFTQLKNKE AELNQKAQKI AEDWAHLKQN KHHHADLEIF LEGEFNHLQQ
     EKHKLLEART QFDNRVSLLS ARFKQKQAEL VKQKQSLEQL TAAFNKEQEA VERDWKDRLA
     NLEKQKEMLG DKVHQFDENS LNISKKLAER ELAIKFKEKE LEAAQKQLSL DNNNNAGLKL
     QLDKLSESLK TERLELEASK ERILDFYDES SRRIADYESD LQARLAEVKT LEKNQQETAA
     KSERELKVAL EKLNQAKKAF LQIRKQQLLE IASVKQQLAQ KANLLKNQQA ELDKQTEELE
     AAFLEQDTDK KELEKALHSV KSKQELLERE RSFLLQKQRE FAEHVAGFKR QVHFKTTQMQ
     RLSEFNKQQQ SEQIKRETEL KIAFADLKKD YQLFELQKNQ EFQQIEQKHK ELELLAQKQA
     ELKQELEQKA TALASQDQDT VQAKLDLARQ QHELELRQNA FNQASLSLNK QREQLTNQVK
     VLHGELKKRH EKLTLKDRLL AEKEKDQHKK DAEINQRFKQ FENEYADFDQ AKKRELQELN
     QIRRNLEQSN ASLLKKRNQL TLDFALLRKV QHNTQTNRVQ LNTQIKEFLL EKKNFQKASD
     EAALQKALLI KRLRSFASKL QLQREALAIQ KLEFDKRDEQ QKSEINNAKL QLEQFKLEKQ
     NFDEAKQKQL IEFKDQCQRL DVEKRLLKQK LVQLKNLSKS YLTYKNRADL SQQQLQHKYA
     NLLELKEKLQ TAKRALDKKH RAIYGKMAQF VSELRQEKKQ LLSAQKQVDD KSRLLEQNQR
     HLQNLSSETK KKRQSLEHDI NKFDQRRKEA VSSILNSHKK LKQKEGELQG ILQKLSLKKT
     QIEQEFSKLY QQREKLDRQR TTLSKLHREL KAQNEATAHK NREVLEIENY YKKELQRLTT
     EKSEFDNNKN RLFEYFRKIR NEIEKKEAHI KTVLEETQKK RHLVETEAVK LHLQKQSIIS
     KGQELKEIKE RVSRDISHTN KQREELNSLL HQNKLLQKNL AEREREINNK DSLLTQKIQT
     AKQKLSEKEA RILKLLEKMR AVEQQYQAEI TRLKTRNADL EKNDNKHLFP PLFKINGNDM
     NYPYPYPWFY PQQKQEDSSN QIRHLFEQQL QFMQQRYENE LTELRRQRAL LEKKLDQIQL
     ESQLSAKKND FEKVEQMMQK LLEKTEQKLS AFDQKINALA EQINTQKAEH ADSEKQQLLL
     RIEQLEKQNL AQAVQTPQPV QPVVQAPAVV PQVIQPQVVQ SQPAFLATQQ SISKQQQIAQ
     LNAEINSIKK LIAQKAAK