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PMPC_CHLTR
ID   PMPC_CHLTR              Reviewed;        1770 AA.
AC   O84419;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Probable outer membrane protein PmpC;
DE   AltName: Full=Polymorphic membrane protein C;
DE   Flags: Precursor;
GN   Name=pmpC; OrderedLocusNames=CT_414;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall. Cell outer membrane
CC       {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Extracellular
CC       side {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Elementary body.
CC   -!- SIMILARITY: Belongs to the PMP outer membrane protein family.
CC       {ECO:0000305}.
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DR   EMBL; AE001273; AAC68011.1; -; Genomic_DNA.
DR   PIR; A71517; A71517.
DR   RefSeq; NP_219924.1; NC_000117.1.
DR   RefSeq; WP_010725193.1; NC_000117.1.
DR   AlphaFoldDB; O84419; -.
DR   STRING; 813.O172_02245; -.
DR   EnsemblBacteria; AAC68011; AAC68011; CT_414.
DR   GeneID; 884702; -.
DR   KEGG; ctr:CT_414; -.
DR   PATRIC; fig|272561.5.peg.445; -.
DR   HOGENOM; CLU_001452_0_0_0; -.
DR   InParanoid; O84419; -.
DR   OMA; NETHPAQ; -.
DR   Proteomes; UP000000431; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR   GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR   Gene3D; 2.40.128.130; -; 1.
DR   InterPro; IPR005546; Autotransporte_beta.
DR   InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR011427; Polymorphic_membr_middle.
DR   InterPro; IPR003368; POMP_repeat.
DR   Pfam; PF03797; Autotransporter; 1.
DR   Pfam; PF02415; Chlam_PMP; 1.
DR   Pfam; PF07548; ChlamPMP_M; 1.
DR   SMART; SM00869; Autotransporter; 1.
DR   SUPFAM; SSF103515; SSF103515; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
DR   TIGRFAMs; TIGR01376; POMP_repeat; 6.
DR   PROSITE; PS51208; AUTOTRANSPORTER; 1.
PE   2: Evidence at transcript level;
KW   Cell outer membrane; Cell wall; Membrane; Reference proteome; Secreted;
KW   Signal; Transmembrane; Transmembrane beta strand.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..1770
FT                   /note="Probable outer membrane protein PmpC"
FT                   /id="PRO_0000024721"
FT   DOMAIN          1477..1770
FT                   /note="Autotransporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT   REGION          73..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          264..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          481..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          611..818
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1271..1329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..97
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..301
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..505
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        629..704
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        705..719
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        720..818
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1277..1329
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1770 AA;  186966 MW;  6FB918F3DBF3E3C4 CRC64;
     MKFMSATAVF AAALSSVTEA SSIQDQIKNT DCNVSKLGYS TSQAFTDMML ADNTEYRAAD
     SVSFYDFSTS SRLPRKHLSS SSEASPTTEG VSSSSSGETD EKTEEELDNG GIIYAREKLT
     ISESQDSLSN QSIELHDNSI FFGEGEVIFD HRVALKNGGA IYGEKEVVFE NIKSLLVEVN
     IAVEKGGSVY AKERVSLENV TEATFSSNGG EQGGGGIYSE QDMLISDCNN VHFQGNAAGA
     TAVKQCLDEE MIVLLAECVD SLSEDTLDST PETEQTESNG NQDGSSETED TQVSESPEST
     PSPDDVLGKG GGIYTEKSLT ITGITGTIDF VSNIATDSGA GVFTKENLSC TNTNSLQFLK
     NSAGQHGGGA YVTQTMSVTN TTSESITTPP LIGEVIFSEN TAKGHGGGIC TNKLSLSNLK
     TVTLTKNSAK ESGGAIFTDL ASIPITDTPE SSTPSSSSPA STPEVVASAK INRFFASTAK
     PAAPSLTEAE SDQTDQTETS DTNSDIDVSI ENILNVAINQ NTSAKKGGAI YGKKAKLSRI
     NNLELSGNSS QDVGGGLCLT ESVEFDAIGS LLSHYNSAAK EGGAIHSKTV TLSNLKSTFT
     FADNTVKAIV ESTPEAPEEI PPVEGEESTA TEDPNSNTEG SSANTNLEGS QGDTADTGTG
     DVNNESQDTS DTGNAESEEQ LQDSTQSNEE NTLPNSNIDQ SNENTDESSD SHTEEITDES
     VSSSSESGSS TPQDGGAASS GAPSGDQSIS ANACLAKSYA ASTDSSPVSN SSGSEEPVTS
     SSDSDVTASS DNPDSSSSGD SAGDSEEPTE PEAGSTTETL TLIGGGAIYG ETVKIENFSG
     QGIFSGNKAI DNTTEGSSSK SDVLGGAVYA KTLFNLDSGS SRRTVTFSGN TVSSQSTTGQ
     VAGGAIYSPT VTIATPVVFS KNSATNNANN TTDTQRKDTF GGAIGATSAV SLSGGAHFLE
     NVADLGSAIG LVPGTQNTET VKLESGSYYF EKNKALKRAT IYAPVVSIKA YTATFNQNRS
     LEEGSAIYFT KEASIESLGS VLFTGNLVTL TLSTTTEGTP ATTSGDVTKY GAAIFGQIAS
     SNGSQTDNLP LKLIASGGNI CFRNNEYRPT SSDTGTSTFC SIAGDVKLTM QAAKGKTISF
     FDAIRTSTKK TGTQATAYDT LDINKSEDSE TVNSAFTGTI LFSSELHENK SYIPQNVVLH
     SGSLVLKPNT ELHVISFEQK EGSSLVMTPG SVLSNQTVAD GALVINNMTI DLSSVEKNGI
     AEGNIFTPPE LRIIDTTTGG SGGTPSTDSE SNQNSDDTEE QNNNDASNQG ESANGSSSPA
     VAAAHTSRTR NFAAAATATP TTTPTATTTT SNQVILGGEI KLIDPNGTFF QNPALRSDQQ
     ISLLVLPTDS SKMQAQKIVL TGDIAPQKGY TGTLTLDPDQ LQNGTISVLW KFDSYRQWAY
     VPRDNHFYAN SILGSQMLMV TVKQGLLNDK MNLARFEEVS YNNLWISGLG TMLSQVGTPT
     SEEFTYYSRG ASVALDAKPA HDVIVGAAFS KMIGKTKSLK RENNYTHKGS EYSYQASVYG
     GKPFHFVINK KTEKSLPLLL QGVISYGYIK HDTVTHYPTI RERNKGEWED LGWLTALRVS
     SVLRTPAQGD TKRITVYGEL EYSSIRQKQF TETEYDPRYF DNCTYRNLAI PMGLAFEGEL
     SGNDILMYNR FSVAYMLSIY RNSPTCKYQV LSSGEGGEII CGVPTRNSAR GEYSTQLYLG
     PLWTLYGSYT IEADAHTLAH MMNCGARMTF
 
 
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