ID Q2TGL3_CHLTH Unreviewed; 1751 AA.
AC Q2TGL3;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 13-SEP-2023, entry version 49.
DE SubName: Full=Polymorphic membrane protein B {ECO:0000313|EMBL:AAX76538.1};
GN Name=pmpB {ECO:0000313|EMBL:AAX76538.1};
OS Chlamydia trachomatis.
OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=813 {ECO:0000313|EMBL:AAX76538.1};
RN [1] {ECO:0000313|EMBL:AAX76538.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UW-36 {ECO:0000313|EMBL:AAX76538.1};
RX PubMed=16352844; DOI=10.1128/JB.188.1.275-286.2006;
RA Gomes J.P., Nunes A., Bruno W.J., Borrego M.J., Florindo C., Dean D.;
RT "Polymorphisms in the nine polymorphic membrane proteins of Chlamydia
RT trachomatis across all serovars: evidence for serovar Da recombination and
RT correlation with tissue tropism.";
RL J. Bacteriol. 188:275-286(2006).
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; AY884121; AAX76538.1; -; Genomic_DNA.
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; IPR006626; PbH1.
DR InterPro; IPR011427; Polymorphic_membr_middle.
DR InterPro; IPR003368; POMP_repeat.
DR NCBIfam; TIGR01376; POMP_repeat; 6.
DR PANTHER; PTHR19862; WD REPEAT-CONTAINING PROTEIN 48; 1.
DR PANTHER; PTHR19862:SF14; WD REPEAT-CONTAINING PROTEIN 48; 1.
DR Pfam; PF03797; Autotransporter; 1.
DR Pfam; PF02415; Chlam_PMP; 5.
DR Pfam; PF07548; ChlamPMP_M; 1.
DR SMART; SM00869; Autotransporter; 1.
DR SMART; SM00710; PbH1; 9.
DR SUPFAM; SSF103515; Autotransporter; 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};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane beta strand {ECO:0000256|ARBA:ARBA00022452}.
FT DOMAIN 1458..1751
FT /note="Autotransporter"
FT /evidence="ECO:0000259|PROSITE:PS51208"
FT REGION 65..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1296..1329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1751 AA; 183045 MW; 7382910F5B08DCDF CRC64;
MKWLSATAVF AAVLPSVSGF CFPEPKELNF SRVGTSSSTT FTETVGEAGA EYIVSGNASF
TKFTNIPTTD TTTPTNSNSS SSNGETASVS EDSDSTTTTP DPKGGGAFYN AHSGVLSFMT
RSGTEGSLTL SEIKMTGEGG AIFSQGELLF TDLTGLTIQN NLSQLSGGAI FGGSTISLSG
ITKATFSSNS AEVPAPVKKP TEPKAQTASE TSGSSSSSGN DSVSSPSSSR AEPAAANLQS
HFICATATPA AQTDTETSTP SHKPGSGGAI YAKGDLTIAD SQEVLFSINK ATKDGGAIFA
EKDVSFENIT SLKVQTNGAE EKGGAIYAKG DLSIQSSKQS LFNSNYSKQG GGALYVEGDI
NFQDLEEIRI KYNKAGTFET KKITLPKAQA SAGNADAWAS SSPQSGSGAT TVSNSGDSSS
GSDSDTSETV PATAKGGGLY TDKNLSITNI TGIIEIANNK ATDVGGGAYV KGTLTCENSH
RLQFLKNSSD KQGGGIYGED NITLSNLTGK TLFQENTAKE EGGGLFIKGT DKALTMTGLD
SFCLINNTSE KHGGGAFVTK EISQTYTSDV ETIPGITPVH GETVITGNKS TGGNGGGVCT
KRLALSNLQS ISISGNSAAE NGGGAHTCPD SFPTADTAEQ PAAASAATST PKSAPVVSTA
LSTPSSSTVS SLTLLAASSQ ASPATSNKET QDPNADTDLL IDYVVDTTIS KNTAKKGGGI
YAKKAKMSRI DQLNISENSA TEIGGGICCK ESLELDTLVS LSVTENLVGK EGGGLHAKTV
NISNLKSGFS FSNNKANSSS TGVATTASAP AAAAASLQAA AAAAPTSPAT PTYSGVVGGA
IYGEKVTFSQ CSGTCQFSGN QAIDNNPSQS SLNVQGGAIY AKTSLSIGSS DAGTSYIFSG
NSVSTGKSQT TGQIAGGAIY SPTVTLNCPA TFSNNTASMA TPKTSSEDGS SGNSIKDTIG
GAIAGTAITL SGVSRFSGNT ADLGAAIGTL ANANTPSATS GSQNSITEKI TLENGSFIFE
RNQANKRGAI YSPSVSIKGN NITFNQNTST HDGSAIYFTK DATIESLGSV LFTGNNVTAT
QASSATSGQN TNTANYGAAI FGDPGTTQSS QTDAILTLLA SSGNITFSNN SLQNNQGDTP
ASKFCSIAGY VKLSLQAAKG KTISFFDCVH TSTKKTGSTQ KVYETLDINK EEKSNPYTGT
IVFSSELHEN KSYIPQNAIL HNGTLVLKEK TELHVVSFEQ KEGSKLIMEP GAVLSNQNIA
NGALAINGLT IDLSSMGTPQ AGEIFSPPEL RIVATTSSAS GGSGVSSSIP TNPKRISAAA
PSGSAATTPT MSENKVFLTG DLTLIDPNRN FYQNPILGSD LDVPLIKLPT DTSDVQVYDL
TLSGDLFPQK GYMGTWTLDS NPQTGKLQAR WTFDTYRRWV YIPRDNHFYA NSILGSQNSM
IVVKQGLINN MLNNARFDDI AYNNFWVSGV GTFLAQQGTP LSEEFSYYSR GTSVAIDAKP
RQDFILGAAF SKMVGKTKAI KKMHNYFHKG SEYSYQASVY GGKFLYFLLN KQHGWALPFL
IQGVVSYGHI KHDTTTLYPS IHERNKGDWE DLGWLADLRI SMDLKEPSKD SSKRITVYGE
LEYSSIRQKQ FTEIDYDPRH FDDCAYRNLS LPVGCAVEGA IMNCNILMYN KLALAYMPSI
YRNNPVCKYR VLSSNEAGQV ICGVPTRTSA RAEYSTQLYL GPFWTLYGNY TIDVGMYTLS
QMTSCGARMI F
//
