ID Q6HA44_CHLTH Unreviewed; 1770 AA.
AC Q6HA44;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Polymorphic membrane protein C {ECO:0000313|EMBL:AAQ08588.1};
GN Name=pmpC {ECO:0000313|EMBL:AAQ08588.1};
OS Chlamydia trachomatis.
OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=813 {ECO:0000313|EMBL:AAQ08588.1};
RN [1] {ECO:0000313|EMBL:AAQ08588.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UW-12 {ECO:0000313|EMBL:AAQ08588.1};
RX PubMed=15205432; DOI=10.1128/JB.186.13.4295-4306.2004;
RA Gomes J.P., Bruno W.J., Borrego M.J., Dean D.;
RT "Recombination in the genome of Chlamydia trachomatis involving the
RT polymorphic membrane protein C gene relative to ompA and evidence for
RT horizontal gene transfer.";
RL J. Bacteriol. 186:4295-4306(2004).
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000256|ARBA:ARBA00004416}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004416}; Extracellular side
CC {ECO:0000256|ARBA:ARBA00004416}. Secreted, cell wall
CC {ECO:0000256|ARBA:ARBA00004191}.
CC -!- SIMILARITY: Belongs to the PMP outer membrane protein family.
CC {ECO:0000256|ARBA:ARBA00007542}.
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DR EMBL; AF519757; AAQ08588.1; -; Genomic_DNA.
DR RefSeq; WP_055348943.1; NZ_CP017746.1.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR Gene3D; 2.40.128.130; Autotransporter beta-domain; 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 NCBIfam; TIGR01376; POMP_repeat; 6.
DR PANTHER; PTHR13491; ZCCHC10 PROTEIN; 1.
DR PANTHER; PTHR13491:SF0; ZINC FINGER CCHC DOMAIN-CONTAINING PROTEIN 10; 1.
DR Pfam; PF03797; Autotransporter; 1.
DR Pfam; PF02415; Chlam_PMP; 4.
DR Pfam; PF07548; ChlamPMP_M; 1.
DR SMART; SM00869; Autotransporter; 1.
DR SUPFAM; SSF103515; Autotransporter; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS51208; AUTOTRANSPORTER; 1.
PE 3: Inferred from homology;
KW Cell outer membrane {ECO:0000256|ARBA:ARBA00023237};
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane beta strand {ECO:0000256|ARBA:ARBA00022452}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1770
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030175976"
FT DOMAIN 1477..1770
FT /note="Autotransporter"
FT /evidence="ECO:0000259|PROSITE:PS51208"
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..824
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..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1770 AA; 186805 MW; 14450AD1E67734F0 CRC64;
MKFMSATAVF AAALSSVTEA SSIQDQIKNT DCNVSKVGYS 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 LVGEVIFSEN 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 DTGNAESGEQ LQDSTQSNEE NALPNSNIDQ SNENTDESSD SYTEEITDES
VSSSSESGSS TPQDGGAASS GAPSGDQSIS ANACLAKSYA ASTDSSPVSN SSGSEEPVTS
SSDSDVTASS DNPDSSSSGD SAGNSEEPTE PEAGSTTETP TLIGGGAIYG ETVKIENFSG
QGIFSGNKAI DNTTEGSSSK SDVLGGAVYA KTLFNLDSGS SRRTVTFSGN TVSSQSTTGQ
VAGGAIYSPT VTIATPVVFS KNSATNNANN ATDTQRKDTF GGAIGATSTV 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 LRIIDTTTSG SGGTPSTDSE SNQNSDDTEE QNNNDASNQG ESANGSSSPA
VAAAHTSRTR NFAAAATATP TTTPTATTTT SNQVILGGEI KLIDPNGTFF QNPALRSDQQ
ISLLVLPTDS SKMQAQKIVL TGDIAPQKGY TGTLTLDPDQ LQNGTISVLW KFDSYRQWAY
VPRDNHFYAN SILGSQMSMV TVKQGLLNDK MNLARFEEVS YNNLWISGLG TMLSQVGTPT
SEEFTYYSRG ASVALDAKPA HDVIVGAAFS KMIGKTKSLK RENNYTHKGS EYSYQASVYG
GKPFHFVINK KTEKSLPLLL QGVISYGYIK HDTVTHYPTI RERNKGEWED LGWLTALRVS
SVLKTPAQGD TKRITVYGEL EYSSIRQKQF TETEYDPRYF DNCTYRNLAI PMGLAFEGEL
SGNDILMYNR FSVAYMPSIY RNSPTCKYQV LSSGEGGEII CGVPTRNSAR GEYSTQLYLG
PLWTLYGSYT IEADAHTLAH MMNCGARMTF
//
