ID   HMW3_MYCGA              Reviewed;        1076 AA.
AC   Q7NBT3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Cytadherence high molecular weight protein 3;
DE   AltName: Full=Accessory adhesin protein 3;
DE   AltName: Full=Cytadherence accessory protein 3;
GN   Name=hlp3; Synonyms=hmw3; OrderedLocusNames=MYCGA1770; ORFNames=MGA_0928;
OS   Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS   (Mycoplasmoides gallisepticum).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=710127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R(low / passage 15 / clone 2);
RX   PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA   Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA   Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT   "The complete genome sequence of the avian pathogen Mycoplasma
RT   gallisepticum strain R(low).";
RL   Microbiology 149:2307-2316(2003).
RN   [2]
RP   PROTEIN SEQUENCE OF 621-627, AND FIBRONECTIN-BINDING.
RC   STRAIN=R(high / passage 164), and R(low / passage 14);
RX   PubMed=16495551; DOI=10.1128/iai.74.3.1777-1785.2006;
RA   May M., Papazisi L., Gorton T.S., Geary S.J.;
RT   "Identification of fibronectin-binding proteins in Mycoplasma gallisepticum
RT   strain R.";
RL   Infect. Immun. 74:1777-1785(2006).
CC   -!- FUNCTION: Binds immobilized fibronectin.
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. Essential for successful surface parasitism (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, attachment organelle membrane
CC       {ECO:0000250}. Note=Localizes specifically to the attachment membrane.
CC       {ECO:0000250}.
CC   -!- POLYMORPHISM: Runs as a smaller protein in high passage extracts
CC       (passage 164) versus low passage (passage 14) that shares the same N-
CC       terminus. Sequencing has shown this smaller version to be due to an
CC       internal 54 bp deletion.
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DR   EMBL; AE015450; AAP56527.2; -; Genomic_DNA.
DR   RefSeq; WP_011113409.1; NC_004829.2.
DR   AlphaFoldDB; Q7NBT3; -.
DR   SMR; Q7NBT3; -.
DR   KEGG; mga:MGA_0928; -.
DR   PATRIC; fig|233150.7.peg.194; -.
DR   HOGENOM; CLU_289644_0_0_14; -.
DR   OrthoDB; 10737at544448; -.
DR   Proteomes; UP000001418; Chromosome.
DR   GO; GO:0033111; C:attachment organelle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020035; P:adhesion of symbiont to microvasculature; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell projection; Coiled coil; Cytadherence;
KW   Direct protein sequencing; Membrane; Reference proteome; Virulence.
FT   CHAIN           1..1076
FT                   /note="Cytadherence high molecular weight protein 3"
FT                   /id="PRO_0000380121"
FT   REGION          264..284
FT                   /note="Fibronectin-binding"
FT   REGION          326..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          789..808
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          850..873
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          562..616
FT                   /evidence="ECO:0000255"
FT   VARIANT         265..282
FT                   /note="Missing (in high passage 164 isolate)"
SQ   SEQUENCE   1076 AA;  126432 MW;  45CA5C7C52D00263 CRC64;
     MIMNPKIHNK ILKNLAKLKK KVFTKYAAYD FNFAYDKNGN VYLVGVDNVT NQTFNLIKPV
     FKFLKKPLPA ELYGMDQQPF YFVNNHHYID ALNSDTGEQE LLRYNVIDQS LVNAQTNDLV
     DPAFYTDLEG YELDLSQYTG SLLDLSNEVI SVEQQPVEQE VNLTPEQVEE AEQVEQQPVD
     QQQVQQVDPN LNEQPVEGDN QNFTQQYYDQ QLGYADQNVD YGYDPQQYTQ EQDYVDNTQQ
     YDQVQDYVDP NQQYYDDQQQ YDQQGYDQGY DQQYDQQGYD QQGYDQGYDQ QYDQQYYDDQ
     QQYDEQPDQQ VKAVVEQVVD EVVEEQQPVE VAKPAPTKPV GPKPQPGKKA TKYVIKKPEP
     KPKVVKEEPI EPAVEKEEVV TVVEQVVDQP VQVAEVQPEP VVVADDEIKL ASEQPVKKKI
     NLDDLQQIPV VIKLPKFETP KLPEPKADSE QKEEIAVKVV EQPVENPQVQ ETKHHHALPK
     VKIEKRQEVE LVPSKLDDHY DLIEEEDDFF VDKFKFEDIK LSDLLVEQKP IEVNQPVQQP
     VVLEQSTPSV QAQPQSVEPK LEITKLEELV EIKTDNTESL NKLETLIDEN KKIIDQFKQL
     KEEAKKSNSN INLEKVAKQL VDYLTNKLNE KTAALNKPEP STVELNKVEQ AKQKAVEKLV
     HEQVVFQPRE KVVQQPKEVV AKPYFEESDD LLTSVSNKPK QPTSELLDFL VQQVVDGEED
     DLPPPTNFDK WPNQNVRQKL DEINQVEAQR FNQTQFVPPQ SLNQVETPNQ RLFLEPEIQV
     QPQALYTASR EHEQVQPKAQ HQQPTTRIER EEVVNKFQRE PLVSPNRLAY HSNKEFDDLY
     QNHYEQRTAR INPQDSYYDQ GYEQPDPYQE QQPYPQEQYL DPRYQQQVDP RYQKETYQEY
     NRPFPPNQEY DYYPPAYESR RDYQPYQPRR VNYEVRKPLA YEFSKQPAPR RYQQLPNRYN
     ESDQSRQLAY PVHKGTLRTE ADFLRFREGY GYDYDRPSTQ YYRSNYDTYV REVRRPIRQL
     GMIEPVAEFR SRTLAPRRVA RPTYGLRRVS RIPSLAPRGY NQQPRVRRVP VSRGYW